ID RSXB_ECOLI Reviewed; 192 AA. AC P77223; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 175. 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=Rsx electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000305}; GN Name=rsxB {ECO:0000255|HAMAP-Rule:MF_00463, GN ECO:0000303|PubMed:12773378}; Synonyms=rnfB, ydgM; GN OrderedLocusNames=b1628, JW1620; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP FUNCTION, SUBUNIT, AND GENE NAME. RX PubMed=12773378; DOI=10.1093/emboj/cdg252; RA Koo M.S., Lee J.H., Rah S.Y., Yeo W.S., Lee J.W., Lee K.L., Koh Y.S., RA Kang S.O., Roe J.H.; RT "A reducing system of the superoxide sensor SoxR in Escherichia coli."; RL EMBO J. 22:2614-2622(2003). CC -!- FUNCTION: Part of a membrane-bound complex that couples electron CC transfer with translocation of ions across the membrane (By CC similarity). Required to maintain the reduced state of SoxR. Probably CC transfers electron from NAD(P)H to SoxR (PubMed:12773378). CC {ECO:0000255|HAMAP-Rule:MF_00463, ECO:0000269|PubMed:12773378}. 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: RsxA, RsxB, RsxC, CC RsxD, RsxE and RsxG. {ECO:0000255|HAMAP-Rule:MF_00463, CC ECO:0000305|PubMed:12773378}. 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; U00096; AAC74700.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15383.1; -; Genomic_DNA. DR PIR; F64919; F64919. DR RefSeq; NP_416145.1; NC_000913.3. DR RefSeq; WP_000991805.1; NZ_SSZK01000001.1. DR AlphaFoldDB; P77223; -. DR BioGRID; 4261721; 47. DR IntAct; P77223; 1. DR STRING; 511145.b1628; -. DR TCDB; 3.D.6.1.4; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family. DR PaxDb; 511145-b1628; -. DR EnsemblBacteria; AAC74700; AAC74700; b1628. DR GeneID; 946146; -. DR KEGG; ecj:JW1620; -. DR KEGG; eco:b1628; -. DR PATRIC; fig|1411691.4.peg.633; -. DR EchoBASE; EB3693; -. DR eggNOG; COG2878; Bacteria. DR HOGENOM; CLU_063448_2_0_6; -. DR InParanoid; P77223; -. DR OMA; KVEGDPI; -. DR OrthoDB; 9789936at2; -. DR PhylomeDB; P77223; -. DR BioCyc; EcoCyc:G6872-MONOMER; -. DR PRO; PR:P77223; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; 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; PTHR43560; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1. DR PANTHER; PTHR43560:SF1; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 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 1: Evidence at protein level; 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..192 FT /note="Ion-translocating oxidoreductase complex subunit B" FT /id="PRO_0000216271" FT DOMAIN 32..91 FT /note="4Fe-4S" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463" FT DOMAIN 108..137 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00463" FT DOMAIN 138..167 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 74 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 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 123 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 127 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 153 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 157 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 192 AA; 20544 MW; 69EC54592EACB7B4 CRC64; MNAIWIAVAA VSLLGLAFGA ILGYASRRFA VEDDPVVEKI DEILPQSQCG QCGYPGCRPY AEAISCNGEK INRCAPGGEA VMLKIAELLN VEPQPLDGEA QEITPARMVA VIDENNCIGC TKCIQACPVD AIVGATRAMH TVMSDLCTGC NLCVDPCPTH CISLQPVAET PDSWKWDLNT IPVRIIPVEH HA //