ID RNFB_BUCAI Reviewed; 167 AA. AC P57214; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 124. 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=BU114; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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}. 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; BA000003; BAB12832.1; -; Genomic_DNA. DR RefSeq; NP_239946.1; NC_002528.1. DR RefSeq; WP_010895952.1; NC_002528.1. DR AlphaFoldDB; P57214; -. DR SMR; P57214; -. DR STRING; 563178.BUAP5A_112; -. DR EnsemblBacteria; BAB12832; BAB12832; BAB12832. DR KEGG; buc:BU114; -. DR PATRIC; fig|107806.10.peg.121; -. DR eggNOG; COG2878; Bacteria. DR HOGENOM; CLU_063448_2_0_6; -. DR BioCyc; BAPH107806:GBZJ-113-MONOMER; -. DR Proteomes; UP000001806; 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 InterPro; IPR016463; RnfB/RsxB_Proteobac. DR NCBIfam; TIGR01944; rnfB; 1. DR PANTHER; PTHR42859:SF3; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1. DR PANTHER; PTHR42859; OXIDOREDUCTASE; 1. DR Pfam; PF14697; Fer4_21; 1. DR Pfam; PF04060; FeS; 1. DR PIRSF; PIRSF005784; Elect_transpt_RnfB; 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; 2. PE 3: Inferred from homology; KW 4Fe-4S; Cell inner membrane; Cell membrane; Electron transport; Iron; KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat; KW Translocase; Transport. FT CHAIN 1..167 FT /note="Ion-translocating oxidoreductase complex subunit B" FT /id="PRO_0000216268" FT DOMAIN 28..87 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..22 FT /note="Hydrophobic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463" FT BINDING 45 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 48 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 53 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 70 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 167 AA; 18333 MW; D9DC969A3C3868A1 CRC64; MITLIIFSFL SFLLGIILSF TAYKFRSQED PIVAIVNELL PQSQCAQCGY SGCYPYAKAI VENSEKINKC IPGGTDLISA ISSVLSIEVP EKNLIITHKK QKNNTVLINE SNCVGCSKCA SFCPVDAIVG APNFIHTVLQ EFCTGCNICL LHCPTNCIEI KKETYEE //