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Database: UniProt
Entry: A1ABH4
LinkDB: A1ABH4
Original site: A1ABH4 
ID   RSXC_ECOK1              Reviewed;         708 AA.
AC   A1ABH4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   01-OCT-2014, entry version 68.
DE   RecName: Full=Electron transport complex subunit RsxC {ECO:0000255|HAMAP-Rule:MF_00461};
GN   Name=rsxC {ECO:0000255|HAMAP-Rule:MF_00461}; Synonyms=rnfC;
GN   OrderedLocusNames=Ecok1_15200; ORFNames=APECO1_712;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- FUNCTION: Part of a membrane complex involved in electron
CC       transport. Required to maintain the reduced state of SoxR.
CC       {ECO:0000255|HAMAP-Rule:MF_00461}.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00461}.
CC   -!- SUBUNIT: Composed of six subunits; RsxA, RsxB, RsxC, RsxD, RsxE
CC       and RsxG. {ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000468; ABJ01014.1; -; Genomic_DNA.
DR   RefSeq; WP_000915715.1; NC_008563.1.
DR   RefSeq; YP_852728.1; NC_008563.1.
DR   ProteinModelPortal; A1ABH4; -.
DR   SMR; A1ABH4; 375-429.
DR   STRING; 405955.APECO1_712; -.
DR   EnsemblBacteria; ABJ01014; ABJ01014; APECO1_712.
DR   GeneID; 4493662; -.
DR   KEGG; ecv:APECO1_712; -.
DR   PATRIC; 18214866; VBIEscCol127180_1712.
DR   eggNOG; COG4656; -.
DR   HOGENOM; HOG000279299; -.
DR   KO; K03615; -.
DR   OMA; QNREESQ; -.
DR   OrthoDB; EOG6W45RX; -.
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:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   HAMAP; MF_00461; RsxC_RnfC; 1.
DR   InterPro; IPR001450; 4Fe4S-bd_dom.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010208; Elect_transpt_cplx_prot_RnfC.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR011538; NADH_UbQ_OxRdtase_51kDa_su.
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   Repeat; Transport.
FT   CHAIN         1    708       Electron transport complex subunit RsxC.
FT                                /FTId=PRO_1000013601.
FT   DOMAIN      369    397       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   DOMAIN      407    436       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       377    377       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       380    380       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       383    383       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       387    387       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       416    416       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       419    419       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       422    422       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
FT   METAL       426    426       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00461}.
SQ   SEQUENCE   708 AA;  76858 MW;  6795070148AA24A4 CRC64;
     MLKLFSAFRK NKIWDFNGGI HPPEMKTQSN GTPLRQVPLA QRFVIPLKQH IGAEGELCVS
     VGDKVLRGQP LTRGRGKMLP VHAPTSGTVT AIAPHSTAHP SALAELSVII DADGEDCWIP
     RDGWADYRSR SREELIERIH QFGVAGLGGA GFPTGVKLQG GGDKIETLII NAAECEPYIT
     ADDRLMQDCA AQVVEGIRIL AHILQPREIL IGIEDNKPQA ISMLRAVLAD SHDISLRVIP
     TKYPSGGAKQ LTYILTGKQV PHGGRSSDIG VLMQNVGTAY AVKRAVIDGE PITERVVTLT
     GEAIARPGNV WARLGTPVRH LLNDAEFCPS ADQMVIMGGP LMGFTLPWLD VPVVKITNCL
     LAPSANELGE PQEEQSCIRC SACADACPAD LLPQQLYWFS KGQQHDKATT HNIADCIECG
     ACAWVCPSNI PLVQYFRQEK AEIAAIRQEE KRAAEAKARF EARQARLERE KAARLERHKS
     AAVQPAAKDK DAIAAALARV KEKQAQATQP IVIKAGERPD NSAIIAAREA RKAQARAKQA
     ELQQTNDAAT VADPRKTAVE AAIARAKARK LEQQQANAEP EEQIDPRKAA VEAAIARAKA
     RKLEQQQANA EPEEQIDPRK AAVEAAIARA KARKLEQQQA NAEPEEQIDP RKAAVEAAIA
     RAKARKLEQQ QANAEPEEQI DPRKAAVAAA IARVQAKKAA QQKVVNED
//
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