ID A0A1H7ZFC0_9PAST Unreviewed; 686 AA.
AC A0A1H7ZFC0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN05444853_12516 {ECO:0000313|EMBL:SEM57272.1};
OS Pasteurella skyensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=97481 {ECO:0000313|EMBL:SEM57272.1, ECO:0000313|Proteomes:UP000198883};
RN [1] {ECO:0000313|Proteomes:UP000198883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24204 {ECO:0000313|Proteomes:UP000198883};
RA Varghese N., Submissions S.;
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 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; FOBN01000025; SEM57272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7ZFC0; -.
DR STRING; 97481.SAMN05444853_12516; -.
DR OrthoDB; 9767754at2; -.
DR Proteomes; UP000198883; 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 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 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};
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 367..399
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 409..438
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 476..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 379
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 382
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 385
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="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT BINDING 418
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 421
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 424
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="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
SQ SEQUENCE 686 AA; 76469 MW; 0808AB72D1827CC2 CRC64;
MKNDAVSRIR QNKLWDFPGG IHPPEMKSQS NQTPIKRLPL PSHFYVPVVQ HSGSAGDLIV
KEGDKVLKGQ PLTQGENFRQ LPVHSPTSGR VIAIGEHIST NINASPELTV VIQADGEDKW
CERCPITDYT QYDSGTIIDK IYQKGVAGLG GAVFSTSSKL HYADTRCELL IINGAECEPY
ITCDDRLMQD YTAEMIEGIE ILQYVLQPQE VVIAIEDNKP NAIKAVRSAL KNAKNIQLRV
IPTKYPSGSS DQLVQVLTGL EIPQSKRTIE MGIVMHNVGT AYAVKRAVMD DEALIERVVT
LTGNRIGQKG NVWARLGTPL NYLLEQVQFE ESKCFPVLIG GPLMGFSVPT LQVPVTKTVN
CVIAPNVDEY SDEELERNCI RCSICSDACP IGLLPQQLYW HSRAKDHDKA KAYNLDACIE
CGICAFVCPS NIPLVQYFRD EKAEIAEIER KEKQSLEAKQ RFEAREARLQ KEKEAREKRI
QEAADKRREQ ISKQQGEDPV QAALARLKAK KEQAQKVEIK AIKTTIAGEP DNSELMALRK
ARRLAKQQQA VTSEQQFAKN ETSQTEQDPR KLAVAQALAR AKAKKEAQQK EQQAVTSEQQ
FTKNETSQTE QDPRKLAVAQ ALARAKAKKE AQQKEQQAVT SEKQSAKTGT TQTEQDPRKL
AVAQAIARAK AKKEAQKNNR KEDDNV
//
