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Database: UniProt
Entry: E4RML6_HALHG
LinkDB: E4RML6_HALHG
Original site: E4RML6_HALHG 
ID   E4RML6_HALHG            Unreviewed;       443 AA.
AC   E4RML6;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 80.
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   OrderedLocusNames=Halsa_1115 {ECO:0000313|EMBL:ADQ14547.1};
OS   Halanaerobium hydrogeniformans (Halanaerobium sp. (strain sapolanicus)).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ14547.1, ECO:0000313|Proteomes:UP000007434};
RN   [1] {ECO:0000313|EMBL:ADQ14547.1, ECO:0000313|Proteomes:UP000007434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.;
RT   "Complete sequence of Halanaerobium sp. sapolanicus.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ14547.1, ECO:0000313|Proteomes:UP000007434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RX   PubMed=21602336; DOI=10.1128/JB.05209-11;
RA   Brown S.D., Begemann M.B., Mormile M.R., Wall J.D., Han C.S., Goodwin L.A.,
RA   Pitluck S., Land M.L., Hauser L.J., Elias D.A.;
RT   "Complete Genome Sequence of the Haloalkaliphilic, Hydrogen Producing
RT   Halanaerobium hydrogenoformans.";
RL   J. Bacteriol. 193:3682-3683(2011).
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; CP002304; ADQ14547.1; -; Genomic_DNA.
DR   RefSeq; WP_013405630.1; NC_014654.1.
DR   AlphaFoldDB; E4RML6; -.
DR   STRING; 656519.Halsa_1115; -.
DR   KEGG; has:Halsa_1115; -.
DR   eggNOG; COG4656; Bacteria.
DR   HOGENOM; CLU_010808_6_0_9; -.
DR   OrthoDB; 9767754at2; -.
DR   Proteomes; UP000007434; 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; 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:UP000007434};
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          360..389
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          399..428
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         369
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         372
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         375
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="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
FT   BINDING         408
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         411
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         414
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="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00461"
SQ   SEQUENCE   443 AA;  48241 MW;  DF14782846397801 CRC64;
     MKALTFKQGI HPAYNKEMTK DKPLKNAERP KEVLIPIKQH IGAPLDLLVK KGDQVNLGQK
     IADSESFVCA PIHASVSGKV KEIRKVTDPG GNAVDAIVIE ASAEKDEKLV SDLEKHQNLD
     NLSPDEIRNI VREAGIVGLG GAMFPTHVKL SVPEDKNVEY VILNGAECEP YLTVDHRVMV
     ERPNAIVFGL KALMKAVNAE KGLIGIEDNK MEAVESMQDA VADEDNIEIK IVETKYPQGG
     EKMLIEALLD REVPVGGLPL DIEVVVNNTS TAAAVADAIR EGKPLIDRSI SITGRGIESP
     CNLIYRIGTK LSDLVEQAGG LKEDAVKVIA GGPMMGAAQK NLDVPAVKGT SGLLVFVADE
     VEEFDPDPCI NCAKCVDHCP MYLMPTTLVR YAKNNMVEKL EEYQILNCIE CGSCSYVCPS
     KIPLVHYLRL GKSQAMAKRR EEK
//
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