ID A0A1T4WMV4_9GAMM Unreviewed; 534 AA.
AC A0A1T4WMV4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=SAMN02745130_01812 {ECO:0000313|EMBL:SKA77951.1};
OS Thiothrix eikelboomii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiothrix.
OX NCBI_TaxID=92487 {ECO:0000313|EMBL:SKA77951.1, ECO:0000313|Proteomes:UP000190460};
RN [1] {ECO:0000313|EMBL:SKA77951.1, ECO:0000313|Proteomes:UP000190460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49788 {ECO:0000313|EMBL:SKA77951.1,
RC ECO:0000313|Proteomes:UP000190460};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00461}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC 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; FUYB01000007; SKA77951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4WMV4; -.
DR STRING; 92487.SAMN02745130_01812; -.
DR OrthoDB; 9767754at2; -.
DR Proteomes; UP000190460; Unassembled WGS sequence.
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; 3.10.20.600; -; 1.
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; PF12838; Fer4_7; 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; 1.
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 inner membrane {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}; Reference proteome {ECO:0000313|Proteomes:UP000190460};
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 375..406
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 415..445
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 481..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 386
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 389
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 392
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 396
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 425
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 428
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 431
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 435
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 534 AA; 58131 MW; 9AA96E760E344795 CRC64;
MLARLRQWWQ HTGGLELKDY HKTASTQQPV RKLSASTAEE IVIPLQQHTG QPPKPIVQAG
DFVYKGQVLA VANGRISVPV HASTSGRIQA LETRPIAHPS GLNDLCVILI PDGQDQWGDQ
GLPPITDYQA VSAECLHQRI SEAGIVGLGG AVFPSAIKLQ RPESSPSPIT TLVINGAECE
PYITCDDMLM REQAAEIIGG CLIMLQVLQE YTPAQGLNCF IGIEDNKPQA IAAMQTAIDQ
ANDPRLKLIP VPTQYPTGGE RQLITLLTGR EVPSGSRPTA IGVLCHNVAT ARAIYQAVVL
GQPLITRYVT VTGQGVVRPQ NFEVPLGMRM QTLIEAAGGY TSKAQRLIMG GSMMGVALPS
DQLPVVKATN CLWVSEPAVS NPPLPCIRCG RCAEACPVNL LPQQMYWYAR ARDLEKVEQQ
HIFDCIECGC CAYVCPSHLP LVDYYRYAKA DIYAQREARA KADLARERHD FHQERIERAK
REKAEKLAKH KAAAQNKTAD TADKQAAIQA ALARAQAKKA QPAPLSTATE DKPA
//
