RSXC_ECO7I
ID RSXC_ECO7I Reviewed; 740 AA.
AC B7NU04;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00461};
DE AltName: Full=Rsx electron transport complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461};
GN Name=rsxC {ECO:0000255|HAMAP-Rule:MF_00461};
GN OrderedLocusNames=ECIAI39_1427;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane. Required to
CC maintain the reduced state of SoxR. {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: The complex is composed of six subunits: RsxA, RsxB, RsxC,
CC RsxD, RsxE 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. RnfC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00461}.
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DR EMBL; CU928164; CAR17560.1; -; Genomic_DNA.
DR RefSeq; WP_000915802.1; NC_011750.1.
DR RefSeq; YP_002407432.1; NC_011750.1.
DR AlphaFoldDB; B7NU04; -.
DR SMR; B7NU04; -.
DR STRING; 585057.ECIAI39_1427; -.
DR EnsemblBacteria; CAR17560; CAR17560; ECIAI39_1427.
DR KEGG; ect:ECIAI39_1427; -.
DR PATRIC; fig|585057.6.peg.1493; -.
DR HOGENOM; CLU_010808_2_1_6; -.
DR OMA; QQLYWYS; -.
DR Proteomes; UP000000749; 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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11540; -; 1.
DR HAMAP; MF_00461; RsxC_RnfC; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010208; Ion_transpt_RnfC/RsxC.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR026902; RnfC_N.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR PANTHER; PTHR43034; PTHR43034; 1.
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; SSF142019; SSF142019; 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; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Repeat; Translocase; Transport.
FT CHAIN 1..740
FT /note="Ion-translocating oxidoreductase complex subunit C"
FT /id="PRO_1000194515"
FT DOMAIN 369..397
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT DOMAIN 407..436
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT REGION 602..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 377
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 380
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 383
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 387
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 416
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 419
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 422
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
FT BINDING 426
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00461"
SQ SEQUENCE 740 AA; 80239 MW; 6A990598604BF5B9 CRC64;
MLKLFSAFRK NKIWDFNGGI HPPEMKTQSN GTPLRQVPLA QRFVIPLKQH IGAEGELCVS
VGDKVLRGQP LTRGRGKMLP VHAPTSGTVT AIAPHSTAHP SALAELSVII DADGEDCWIP
RDGWDDYRSR SREELIERIH KFGVAGLGGA GFPTGVKLQG GGDKIETLII NAAECEPYIT
ADDRLMQDCA AQVVEGIRIL AHILQPREIL IGIEDNKPQA ISMLRAVLAD SHDISLRVIP
TKYPSGGAKQ LTYILTGKQV PHGGRSSDIG VLMQNVGTAY AVKRAVIDGE PITERVVTLT
GEAIARPGNV WARLGTPVRH LLNDAGFCPS ADQMVIMGGP LMGFTLPWLD VPVVKITNCL
LAPSANELGE PQEEQSCIRC SACADACPAD LLPQQLYWFS KGQQHDKATT HNIADCIECG
ACAWVCPSNI PLVQYFRQEK AEIAAIRQEE KRAAEAKARF EARQARLERE KAARLERHKS
AAVQPAAKDK DAIAAALARV KEKQAQATQP IVIKAGERPD NSAIIAAREA RKAQARAKQA
KLQQTNDAAT VADPRKTAVE AAIARAKARK LEQQQANAEP EQQVDPRKAA VEAAIARAKA
RKLEQQQANA EPEQQVDPRK AAVEAAIARA KARKLEQQQA NAEPEQQVDP RKAAVEAAIA
RAKARKLEQQ QANAEPEEQV DPRKAAVEAA IARAKARKLE QKQANAVPEE QVDPRKAAVA
AAIARVQAKK AAQQKVVNED
