ID D7EAC2_METEZ Unreviewed; 290 AA.
AC D7EAC2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=Metev_1963 {ECO:0000313|EMBL:ADI74793.1};
OS Methanohalobium evestigatum (strain ATCC BAA-1072 / DSM 3721 / NBRC 107634
OS / OCM 161 / Z-7303).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanohalobium.
OX NCBI_TaxID=644295 {ECO:0000313|EMBL:ADI74793.1, ECO:0000313|Proteomes:UP000000391};
RN [1] {ECO:0000313|EMBL:ADI74793.1, ECO:0000313|Proteomes:UP000000391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1072 / DSM 3721 / NBRC 107634 / OCM 161 / Z-7303
RC {ECO:0000313|Proteomes:UP000000391};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Anderson I.,
RA Woyke T.;
RT "Complete sequence chromosome of Methanohalobium evestigatum Z-7303.";
RL Submitted (JUN-2010) 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 Rnf complex is probably composed of eight subunits,
CC including RnfA, RnfB, RnfC, RnfD, RnfE and RnfG. {ECO:0000256|HAMAP-
CC Rule:MF_00463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-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; CP002069; ADI74793.1; -; Genomic_DNA.
DR AlphaFoldDB; D7EAC2; -.
DR STRING; 644295.Metev_1963; -.
DR KEGG; mev:Metev_1963; -.
DR HOGENOM; CLU_053470_0_0_2; -.
DR OrthoDB; 23478at2157; -.
DR Proteomes; UP000000391; 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 CDD; cd10549; MtMvhB_like; 1.
DR Gene3D; 3.30.70.20; -; 2.
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 InterPro; IPR049679; Ion_transpt_RnfB_Methano.
DR NCBIfam; TIGR01944; rnfB; 1.
DR NCBIfam; NF041836; rnfB_Methano; 1.
DR PANTHER; PTHR43560; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR PANTHER; PTHR43560:SF1; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF13187; Fer4_9; 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; 4.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00463};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00463};
KW Electron transport {ECO:0000256|HAMAP-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:UP000000391};
KW Repeat {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|HAMAP-Rule:MF_00463}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..94
FT /note="4Fe-4S"
FT /evidence="ECO:0000259|PROSITE:PS51656"
FT DOMAIN 128..163
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 164..193
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 208..237
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 238..267
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..29
FT /note="Hydrophobic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT REGION 267..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
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 55
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 60
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 77
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 139
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 143
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 149
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 153
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 173
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 176
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 179
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 183
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 290 AA; 30558 MW; F3852A94006DBC8B CRC64;
MDFINVIIQS VAVLGGLGFA IGVMLIAASR IFHVETDPLV EEVLEALPGA NCGACGYAGC
SAFAEAVVSE DAPIDGCPVG GFELAQQIGG ILGKEVTQGE KQYPVVRCKG GVNCVNRFDY
VGIQDCNAVM MLSEGEKGCS YGCMGRGTCV RACPFGAITI GEDRLPHINK NLCTSCGLCI
ESCPNDILVF GKESEKVHVR CRSHDKPKAV KAVCTTGCIG CKICEKNCPE DAIKVNNFLA
EIDQEKCTAC GICVEKCPQG TIEMKETGEK TKTSTKQSAD TSETAEADSG
//
