RSXC_ECO24
ID RSXC_ECO24 Reviewed; 740 AA.
AC A7ZM89;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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}; Synonyms=rnfC;
GN OrderedLocusNames=EcE24377A_1837;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV19695.1; -; Genomic_DNA.
DR RefSeq; WP_000915684.1; NC_009801.1.
DR AlphaFoldDB; A7ZM89; -.
DR SMR; A7ZM89; -.
DR EnsemblBacteria; ABV19695; ABV19695; EcE24377A_1837.
DR KEGG; ecw:EcE24377A_1837; -.
DR HOGENOM; CLU_010808_2_1_6; -.
DR OMA; QQLYWYS; -.
DR Proteomes; UP000001122; 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_1000060338"
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..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..714
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; 80218 MW; 9AA3D2DA0502AE8E CRC64;
MLKLFSAFRK NKIWDFNGGI HPPEMKTQSN GTPLRQVPLA QRFVIPLKQH IGAEGELCVS
VGDKVLRGQP LTRGHGKMLP VHAPTSGTVT AIAPHSTAHP SALAELSVII DADGEDCWIP
RDGWADYRTR SREELIERIH QFGVAGLGGA GFPTGVKLQG GGDKIETLII NAAECEPYIT
ADDRLMQDCA AQVVEGIRIL AHILQPREIL IGIEDNKPQA ISMLRAVLAD SNDISLRVIP
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
ELQQTNDAAT VADPRKTAVE AAIARAKARK LEQQQANAEP EEQVDPRKAA VEAAIARAKA
RKLEQQQANA EPEEQVDPRK AAVEAAIARA KARKLEQQQS NAEPEEQVDP RKAAVEAAIA
RAKARKLEQQ QANAEPEEQV DPRKAAVEAA IARAKARKLE QQQTNAEPEE QVDPRKAAVA
AAIARAQAKK AAQQKVVNED
