ID RSXB_ECO57 Reviewed; 192 AA.
AC P58323;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 142.
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=Rsx electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463};
GN Name=rsxB {ECO:0000255|HAMAP-Rule:MF_00463};
GN OrderedLocusNames=Z2634, ECs2337;
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane. Required to
CC maintain the reduced state of SoxR. {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: RsxA, RsxB, RsxC,
CC RsxD, RsxE and RsxG. {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; AE005174; AAG56617.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35760.1; -; Genomic_DNA.
DR PIR; A99921; A99921.
DR PIR; E85769; E85769.
DR RefSeq; NP_310364.1; NC_002695.1.
DR RefSeq; WP_000991809.1; NZ_VOAI01000007.1.
DR AlphaFoldDB; P58323; -.
DR STRING; 155864.Z2634; -.
DR GeneID; 75204473; -.
DR GeneID; 912556; -.
DR KEGG; ece:Z2634; -.
DR KEGG; ecs:ECs_2337; -.
DR PATRIC; fig|386585.9.peg.2446; -.
DR eggNOG; COG2878; Bacteria.
DR HOGENOM; CLU_063448_2_0_6; -.
DR OMA; KVEGDPI; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 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..192
FT /note="Ion-translocating oxidoreductase complex subunit B"
FT /id="PRO_0000216272"
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; 69E9015C7EF9B2E1 CRC64;
MNAIWIAVAA VSLLGLAFGA ILGYASRRFA VEDDPVVEKI DEILPQSQCG QCGYPGCRPY
AEAISCNGEK INRCAPGGEA VMLKIAELLN VEPQPLDGEA QELTPARMVA VIDENNCIGC
TKCIQACPVD AIVGATRAMH TVMSDLCTGC NLCVDPCPTH CISLQPVAET PDSWKWDLNT
IPVRIIPVEH HA
//
