RSXC_SHISS
ID RSXC_SHISS Reviewed; 740 AA.
AC Q3Z1Y4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=SSON_1529;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ88228.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z1Y4; -.
DR SMR; Q3Z1Y4; -.
DR EnsemblBacteria; AAZ88228; AAZ88228; SSON_1529.
DR KEGG; ssn:SSON_1529; -.
DR HOGENOM; CLU_010808_2_1_6; -.
DR OMA; QQLYWYS; -.
DR Proteomes; UP000002529; 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_1000013616"
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..718
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; 80252 MW; 5D94E12888E8DCA1 CRC64;
MLKLFSAFRK NKIWDFNGGI HPPEMKTQSN GTPLRQVPLA QRFVIPLKQH IGAEGELCVS
VGDKVLRGQP LTRGRGKMLP 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 KARKLEQQQT NAEPEEQVDP RKAAVEAAIA
RAKARKLEQQ QANAEPEEQV DPRKAAVEAA IARAKARKLE QQQTNAEPEE QVDPRKAAVA
AAIARAQAKK AAQQKVVNED
