ID A0A1D9FNF7_9CLOT Unreviewed; 444 AA.
AC A0A1D9FNF7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit C {ECO:0000256|HAMAP-Rule:MF_00461};
DE EC=7.-.-.- {ECO:0000256|HAMAP-Rule:MF_00461};
DE AltName: Full=Rnf electron transport complex subunit C {ECO:0000256|HAMAP-Rule:MF_00461};
GN Name=rnfC {ECO:0000256|HAMAP-Rule:MF_00461};
GN ORFNames=BJL90_13870 {ECO:0000313|EMBL:AOY76842.1};
OS Clostridium formicaceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1497 {ECO:0000313|EMBL:AOY76842.1, ECO:0000313|Proteomes:UP000177894};
RN [1] {ECO:0000313|EMBL:AOY76842.1, ECO:0000313|Proteomes:UP000177894}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27076 {ECO:0000313|EMBL:AOY76842.1,
RC ECO:0000313|Proteomes:UP000177894};
RA Bao T., Cheng C., Zhao J., Yang S.-T., Wang J., Wang M.;
RT "Complete Genome Sequence of Acetogen Clostridium formicoaceticum ATCC
RT 27076.";
RL Submitted (OCT-2016) 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.
CC {ECO:0000256|HAMAP-Rule:MF_00461}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00461};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00461};
CC -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000256|HAMAP-Rule:MF_00461}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00461};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00461}.
CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00461}.
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DR EMBL; CP017603; AOY76842.1; -; Genomic_DNA.
DR RefSeq; WP_070969142.1; NZ_CP020559.1.
DR AlphaFoldDB; A0A1D9FNF7; -.
DR STRING; 1497.BJL90_13870; -.
DR KEGG; cfm:BJL90_13870; -.
DR OrthoDB; 9767754at2; -.
DR Proteomes; UP000177894; 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; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 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 NCBIfam; TIGR01945; rnfC; 1.
DR PANTHER; PTHR43034; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT C; 1.
DR PANTHER; PTHR43034:SF2; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT C; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR Pfam; PF13375; RnfC_N; 1.
DR Pfam; PF10531; SLBB; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00461};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00461};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_00461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00461};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00461}; Membrane {ECO:0000256|HAMAP-Rule:MF_00461};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00461};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00461};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_00461};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00461}.
FT DOMAIN 358..389
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 397..426
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 367
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT BINDING 370
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT BINDING 373
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT BINDING 377
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT BINDING 406
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT BINDING 409
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT BINDING 412
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT BINDING 416
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
SQ SEQUENCE 444 AA; 47496 MW; 8AD95EE5B9B447AC CRC64;
MKALTFRGGI HPPEGKESTE HLKIEKAVDP QTVVIPMQQH IGAPCEPIVK VGDTVKVGQK
IGEAQGFVSS PVHASVSGTV KAIMDMPIVT GNEALAVIIE SDGKNEIDPS VASKGDIEAL
QPKEIIDIIK EAGIVGMGGA TFPTHVKLSP PPDKKVDTII LNGAECEPYL TADHRLMLEM
PEDVVYGLKA MMKAVGVKKG YIGIENNKPD AIDVMLKAIK NESDIKVVAL QTKYPQGGEK
QLIYAVTNKE VPSGGLPMDV GVIVSNVGTA AQIAKTIKTG MPLIERVTTV TGKAIKKPRN
LMVKIGTPIK ELIEQCGGYA VTPGKLILGG PMMGIAQHTD EVSAVKGTSG VLVFDKEGAD
LPNPINCIRC GRCVEICPAN LQPVYISENS LSNRMEQAEK YRALDCIECG SCSYVCPSRR
PLLPSIRVAK NQIIAKKREQ KKSN
//
