ID U2RDJ0_9FUSO Unreviewed; 434 AA.
AC U2RDJ0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=HMPREF1984_01628 {ECO:0000313|EMBL:ERK66589.1};
OS Leptotrichia sp. oral taxon 215 str. W9775.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1321779 {ECO:0000313|EMBL:ERK66589.1, ECO:0000313|Proteomes:UP000016640};
RN [1] {ECO:0000313|EMBL:ERK66589.1, ECO:0000313|Proteomes:UP000016640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9775 {ECO:0000313|EMBL:ERK66589.1,
RC ECO:0000313|Proteomes:UP000016640};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERK66589.1}.
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DR EMBL; AWVR01000055; ERK66589.1; -; Genomic_DNA.
DR RefSeq; WP_021766970.1; NZ_KI272843.1.
DR AlphaFoldDB; U2RDJ0; -.
DR STRING; 1321779.HMPREF1984_01628; -.
DR PATRIC; fig|1321779.3.peg.1546; -.
DR eggNOG; COG4656; Bacteria.
DR HOGENOM; CLU_051682_0_0_0; -.
DR OrthoDB; 9767754at2; -.
DR Proteomes; UP000016640; 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; 3.30.70.20; -; 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 SUPFAM; SSF142984; Nqo1 middle 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 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:UP000016640};
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 350..380
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 390..421
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 360
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 363
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 366
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="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT BINDING 399
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 402
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 405
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="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
SQ SEQUENCE 434 AA; 47806 MW; E10A604C4AC0D7CD CRC64;
MNLISGIGKI RLNGKKGLTK NKEIVTIPEP PMIYIPLIIG SSTAFDVHVQ EGDHVCKGTK
LATRTDMYVP IYSPVSGTVK GIEKRMHISG KVQNHLLIEN DFKNEEVVPF SYENPDELSA
EELVAAIKEI GVLGLGGSGF PTYIKYENAK NIDTVLINAV ECEPYLTSDY KIMEKHAKEL
IDGTHFLMKA GHAKKGVIAI KVVNDKLAKK LQEATEGYQN IEVVTVPDAY PMGWERVLIR
ELFKKEYDRF PGEIGIIVNN ATTAIYLSEA LRDKKPITHR IVTISGEGVK NPENVYVPIG
TSVDYIIEKI GGYTENINEM FVLGGGPMMG KSIANDTFVV TTYSNSITVL PKVVEEELPC
LRCGLCVEHC PAKIQPVQIM NLEKQKNTEG VIAACADRCI TCGLCTYICP SKIEVTDWVG
KAKTRVANAR KAGK
//
