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Database: UniProt
Entry: L0DWP3_THIND
LinkDB: L0DWP3_THIND
Original site: L0DWP3_THIND 
ID   L0DWP3_THIND            Unreviewed;       524 AA.
AC   L0DWP3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 71.
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 [H] {ECO:0000313|EMBL:AGA34024.1};
GN   Synonyms=rnfC {ECO:0000256|HAMAP-Rule:MF_00461};
GN   OrderedLocusNames=TVNIR_2381 {ECO:0000313|EMBL:AGA34024.1};
OS   Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA34024.1, ECO:0000313|Proteomes:UP000010809};
RN   [1] {ECO:0000313|Proteomes:UP000010809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC   {ECO:0000313|Proteomes:UP000010809};
RA   Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA   Ravin N.V., Popov V.O.;
RT   "Complete sequence of Thioalkalivibrio nitratireducens.";
RL   Submitted (DEC-2012) 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; CP003989; AGA34024.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0DWP3; -.
DR   STRING; 1255043.TVNIR_2381; -.
DR   KEGG; tni:TVNIR_2381; -.
DR   PATRIC; fig|1255043.3.peg.2403; -.
DR   eggNOG; COG4656; Bacteria.
DR   HOGENOM; CLU_010808_6_2_6; -.
DR   Proteomes; UP000010809; 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   CDD; cd22249; UDM1_RNF168_RNF169-like; 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};
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          366..396
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          404..435
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          466..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         376
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         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         386
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         415
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         425
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   524 AA;  57341 MW;  BB2F771F2207B3A4 CRC64;
     MRTMHLHRFH GGLKLPDHKT ESTVRPLLAL DIPQVLFLPL SQHIGEPAEP LVGPGDTVLK
     GQRIGHANDY IAAHLHAPTS GRVREIAEYP VPHPSGLTAP CIVIEADGDD RWHDDRLRGW
     PDWHERDARS LRERIRDAGI VGLGGAAFPT AVKLNPRPGK AIHTLVVNGA ECEPYISCDD
     TLMRERPKSV LAGVRIVAHL LGVERVLFAV EDNKPEALRA LRDALSSHDR SRIQLVGIPS
     IYPTGGERQL IRVLTGREVP SAGLPADLGI VCHNPGTLKA VADAVLDGHP LISRIVTVTG
     PGVREPRNVE ALIGTPFADL VAAAGGYAPE VNRLVMGGPM MGFAVGDDAV PVIKGTNCLL
     ATRPQDTPEP GPLMPCIRCG ECTRVCPANL LPQQLYWFAK SKNFDAIQDY GLFDCIECGC
     CARVCPSNIP LVQYYRFAKN EIWAREKERQ KADLARERFE FRQLRQQREE QEKAERLARK
     KAAVAKQAPE GEKKAAIDAA LERARAKKAA QTGENPADNG RPDT
//
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