ID A8ZSV7_DESOH Unreviewed; 303 AA.
AC A8ZSV7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 102.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit B {ECO:0000256|HAMAP-Rule:MF_00463};
DE EC=7.-.-.- {ECO:0000256|HAMAP-Rule:MF_00463};
DE AltName: Full=Rnf electron transport complex subunit B {ECO:0000256|HAMAP-Rule:MF_00463};
GN Name=rnfB {ECO:0000256|HAMAP-Rule:MF_00463};
GN OrderedLocusNames=Dole_0311 {ECO:0000313|EMBL:ABW66121.1};
OS Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus
OS oleovorans).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW66121.1, ECO:0000313|Proteomes:UP000008561};
RN [1] {ECO:0000313|EMBL:ABW66121.1, ECO:0000313|Proteomes:UP000008561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3
RC {ECO:0000313|Proteomes:UP000008561};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-2007) 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_00463}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00463};
CC Note=Binds 3 [4Fe-4S] clusters. {ECO:0000256|HAMAP-Rule:MF_00463};
CC -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000256|HAMAP-Rule:MF_00463}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00463}.
CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00463}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00463}.
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DR EMBL; CP000859; ABW66121.1; -; Genomic_DNA.
DR RefSeq; WP_012173740.1; NC_009943.1.
DR AlphaFoldDB; A8ZSV7; -.
DR STRING; 96561.Dole_0311; -.
DR KEGG; dol:Dole_0311; -.
DR eggNOG; COG1143; Bacteria.
DR eggNOG; COG2878; Bacteria.
DR HOGENOM; CLU_053470_0_0_7; -.
DR OMA; MLPGANC; -.
DR OrthoDB; 9789936at2; -.
DR Proteomes; UP000008561; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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; 1.10.15.40; Electron transport complex subunit B, putative Fe-S cluster; 1.
DR HAMAP; MF_00463; RsxB_RnfB; 1.
DR InterPro; IPR007202; 4Fe-4S_dom.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010207; Elect_transpt_cplx_RnfB/RsxB.
DR NCBIfam; TIGR01944; rnfB; 1.
DR PANTHER; PTHR43560; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR PANTHER; PTHR43560:SF1; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF04060; FeS; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS51656; 4FE4S; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00463};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00463};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00463};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_00463};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00463};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00463};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00463, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00463}; Reference proteome {ECO:0000313|Proteomes:UP000008561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00463};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_00463};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00463}.
FT TRANSMEM 6..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..93
FT /note="4Fe-4S"
FT /evidence="ECO:0000259|PROSITE:PS51656"
FT DOMAIN 162..191
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..28
FT /note="Hydrophobic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 171
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 174
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT BINDING 181
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
SQ SEQUENCE 303 AA; 31656 MW; 674F8D841EDEC197 CRC64;
MSAVTIGLAA GTLVGMAVIL TYILGWANVA FYVEVDPRVD AVSKALPGAN CGGCGFVGCG
EYAEAVVMQG APVNKCAPGG ANCAAAIAQI MGVEVGEALP YRPIVHCGAH TKDKHGISDY
RGEQRCVTAN IVADVQGCTY GCLGFGDCVE ACAYDAIHVI NGLAVVDYTA CVGCGACAKA
CPRNIITMTP FKADRVFAVL CSNKDAGKEV KKVCDVGCLG CKACERACGL FAIKDNLSCI
NYDDYDPEHL EDIFKAIDKC PQKGIVLVGK PSEKDMAAVA DKEAPSVVTP DFKTTVDDTE
WRG
//