RNFB_ALIFM
ID RNFB_ALIFM Reviewed; 194 AA.
AC B5FCN4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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}; OrderedLocusNames=VFMJ11_0973;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) 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: Cell inner membrane {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}.
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DR EMBL; CP001139; ACH65814.1; -; Genomic_DNA.
DR RefSeq; WP_005418571.1; NC_011184.1.
DR AlphaFoldDB; B5FCN4; -.
DR EnsemblBacteria; ACH65814; ACH65814; VFMJ11_0973.
DR GeneID; 64240888; -.
DR KEGG; vfm:VFMJ11_0973; -.
DR HOGENOM; CLU_063448_2_0_6; -.
DR OMA; DEENCIG; -.
DR Proteomes; UP000001857; Chromosome I.
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 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; Cell inner membrane; Cell membrane; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Repeat; Translocase; Transport.
FT CHAIN 1..194
FT /note="Ion-translocating oxidoreductase complex subunit B"
FT /id="PRO_1000194503"
FT DOMAIN 32..90
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 105..134
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT DOMAIN 135..164
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463"
FT REGION 1..26
FT /note="Hydrophobic"
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 52
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 57
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 73
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 114
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 117
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 120
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 124
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 144
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 147
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 150
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 154
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 194 AA; 20537 MW; 231D356BF27E3828 CRC64;
MSSILIAVIA IAALALVFGL ILGFASIKFK VESDPIVEQI DAILPQTQCG QCGYPGCKPY
AEAIANGDMI NKCPPGGQAT IEKLADLMGV DVPSSAHDEE KSIKKVAFIH EDMCIGCTKC
IQACPVDAIV GGTKALHTVI ESECTGCDLC VAPCPTDCIE MIPVKTTPDN WKWDLNTIPV
VNISTDQPSK SSEL
