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RSXC_SALPB
ID   RSXC_SALPB              Reviewed;         735 AA.
AC   A9N025;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=SPAB_01863;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX67256.1; -; Genomic_DNA.
DR   RefSeq; WP_000915662.1; NC_010102.1.
DR   AlphaFoldDB; A9N025; -.
DR   SMR; A9N025; -.
DR   KEGG; spq:SPAB_01863; -.
DR   PATRIC; fig|1016998.12.peg.1755; -.
DR   HOGENOM; CLU_010808_2_1_6; -.
DR   OMA; QQLYWYS; -.
DR   BioCyc; SENT1016998:SPAB_RS07560-MON; -.
DR   Proteomes; UP000008556; 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..735
FT                   /note="Ion-translocating oxidoreductase complex subunit C"
FT                   /id="PRO_1000081143"
FT   DOMAIN          368..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          534..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..605
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..667
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   735 AA;  78532 MW;  65B436AC198DD2FC CRC64;
     MLKLFSAFRK DKIWDFDGGI HPPEMKTQSN GTPLRQVPLA PRFVIPLKQH IGAEGELCVS
     VGDRVLRGQA LTRGRGRMLP VHAPTSGTVI AIAPHSTAHP SALAELSVII DADGEDRWIE
     REGWSDYRAH SREALIERIH QYGVAGLGGA GFPTGVKLQG GGDKITTLII NAAECEPYIT
     ADDRLMQDCA AQIVEGIRIL AHILQPREVL IGIEDNKPQA ISMLRAVLAD AHDISLRVIP
     TKYPSGGAKQ LTQILTGKQV PHGGRSSDIG VLMQNVGTAY AVKRAVVDGE PITERVVTLT
     GEAVSRPGNV WARLGTPVRH LLNDAGFCPS ADQMVIMGGP LMGFTLPWLD VPVVKITNCL
     LAPSVTEMGA PQEEKSCIRC SACADACPAD LLPQQLYWFS KGQQHDKATA HHIADCIECG
     ACAWVCPSNI PLVQYFRQEK AEINAIRLEE KRAAEAKARF EARQARLERE KAVRLARHKS
     AAVQPAAKDQ DAIAAALARV KEKQAQATQP VVIQAGSLPD NSAVIAAREA RKAQARAKQA
     AHPVADSALP GDDPRKAAVE AAIARAKARK QEQQAGSEPA EPVDPRKAAV EAAIARAKAR
     KQEQQAGSEP VEAVDPRKAA VEAAIARAKA RKQEQQAGGE PAEAVDPRKA AVEAAIARAK
     ARKQEQQAGS EPAEPAAPRK AAVEAAIARA KARKQEQQAG SEPAEAVDPR KAAVAAAIAR
     VQAKKAAQQQ VVNED
 
 
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