RNFB_CERS4
ID RNFB_CERS4 Reviewed; 188 AA.
AC Q3IXC5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00463};
DE AltName: Full=Rnf electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463};
GN Name=rnfB {ECO:0000255|HAMAP-Rule:MF_00463};
GN OrderedLocusNames=RHOS4_32410, RSP_3193;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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:0000255|HAMAP-Rule:MF_00463}.
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 -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000255|HAMAP-Rule:MF_00463}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00463}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_00463}.
CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000144; ABA80809.1; -; Genomic_DNA.
DR RefSeq; WP_011339116.1; NZ_CP030272.1.
DR RefSeq; YP_354710.1; NC_007494.2.
DR AlphaFoldDB; Q3IXC5; -.
DR STRING; 272943.RSP_3193; -.
DR EnsemblBacteria; ABA80809; ABA80809; RSP_3193.
DR KEGG; rsp:RSP_3193; -.
DR PATRIC; fig|272943.9.peg.3623; -.
DR eggNOG; COG2878; Bacteria.
DR OMA; DEENCIG; -.
DR PhylomeDB; Q3IXC5; -.
DR Proteomes; UP000002703; Chromosome 2.
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 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Nitrogen fixation; Reference proteome; Repeat; Translocase; Transport.
FT CHAIN 1..188
FT /note="Ion-translocating oxidoreductase complex subunit B"
FT /id="PRO_1000194489"
FT DOMAIN 29..88
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 104..133
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 134..163
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 113
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 116
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 119
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 123
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 143
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 146
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 149
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 153
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 188 AA; 19249 MW; 45C9FEFEAE31F20F CRC64;
MIEAAVSMSA LGLGLGLLLG VAARRFHVES PPIVDAIEGI LPGTNCGACG YPGCRGLAEA
MSEGAAPVTA CAPGGRDVAL ALAAIVETDG GGGAVPGMAE AEPTVAFIFE DHCTGCMRCF
KRCPTDAIIG ANRQIHTVVT DACIGCNACI EACPTEAIVA RVKPKTLKSW YWDKPRTAFE
ARGTEVAA
