RNFB_RHOCA
ID RNFB_RHOCA Reviewed; 187 AA.
AC P0CZ14; O08056; Q07394;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305};
DE AltName: Full=Nitrogen fixation protein RnfB {ECO:0000305};
DE AltName: Full=Rnf electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305};
GN Name=rnfB {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000303|PubMed:8264535};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND GENE NAME.
RC STRAIN=B10S;
RX PubMed=8264535; DOI=10.1007/bf00279903;
RA Schmehl M., Jahn A., Meyer zu Vilsendorf A., Hennecke S., Masepohl B.,
RA Schuppler M., Marxer M., Oelze J., Klipp W.;
RT "Identification of a new class of nitrogen fixation genes in Rhodobacter
RT capsulatus: a putative membrane complex involved in electron transport to
RT nitrogenase.";
RL Mol. Gen. Genet. 241:602-615(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, SUBUNIT,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=9492268; DOI=10.1046/j.1432-1327.1998.2510054.x;
RA Jouanneau Y., Jeong H.-S., Hugo N., Meyer C., Willison J.C.;
RT "Overexpression in Escherichia coli of the rnf genes from Rhodobacter
RT capsulatus -- characterization of two membrane-bound iron-sulfur
RT proteins.";
RL Eur. J. Biochem. 251:54-64(1998).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane (By
CC similarity). Required for nitrogen fixation. Involved in electron
CC transfer to nitrogenase (PubMed:8264535). {ECO:0000255|HAMAP-
CC Rule:MF_00463, ECO:0000269|PubMed:8264535}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00463};
CC Note=Binds 3 [4Fe-4S] clusters. {ECO:0000255|HAMAP-Rule:MF_00463};
CC -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00463,
CC ECO:0000305|PubMed:9492268}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000269|PubMed:9492268};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00463,
CC ECO:0000269|PubMed:9492268}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:D5ARZ0, ECO:0000255|HAMAP-Rule:MF_00463}.
CC -!- INDUCTION: Expression is reduced under iron-limiting conditions.
CC {ECO:0000269|PubMed:9492268}.
CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
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DR EMBL; X72888; CAA51400.1; -; Genomic_DNA.
DR EMBL; Y11913; CAA72669.1; -; Genomic_DNA.
DR PIR; S39894; S39894.
DR RefSeq; WP_013068984.1; NZ_VIBE01000016.1.
DR AlphaFoldDB; P0CZ14; -.
DR GeneID; 31492068; -.
DR OMA; DEENCIG; -.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore 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 GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
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; IPR016463; RnfB/RsxB_Proteobac.
DR PANTHER; PTHR42859:SF3; PTHR42859:SF3; 1.
DR Pfam; PF04060; FeS; 1.
DR PIRSF; PIRSF005784; Elect_transpt_RnfB; 1.
DR TIGRFAMs; TIGR01944; rnfB; 1.
DR PROSITE; PS51656; 4FE4S; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Nitrogen fixation; Repeat; Translocase; Transport.
FT CHAIN 1..187
FT /note="Ion-translocating oxidoreductase complex subunit B"
FT /id="PRO_0000216277"
FT DOMAIN 29..88
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 103..132
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 133..162
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT REGION 1..23
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00463"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
SQ SEQUENCE 187 AA; 19090 MW; 93965D368FC63D3F CRC64;
MIAAAASMSA LGLGLGYLLG AAARKFHVET PPIVEEIAKI LPGTNCGACG FPGCNGLAEA
MAEGNAPVTA CTPGGRDVAL ALAEIVTVEA GADAGPIAEI EPMVAFVFED HCTGCQKCFK
RCPTDAIVGG AKQIHTVVMD ACIGCDACIE VCPTEAIVSR VKPKTLKTWY WDKPQPGLVA
ASAETAA
