GenomeNet

Database: UniProt
Entry: Q1RBG8
LinkDB: Q1RBG8
Original site: Q1RBG8 
ID   RSXB_ECOUT              Reviewed;         192 AA.
AC   Q1RBG8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   05-DEC-2018, entry version 88.
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}; Synonyms=rnfB;
GN   OrderedLocusNames=UTI89_C1818;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane. Required
CC       to maintain the reduced state of SoxR. {ECO:0000255|HAMAP-
CC       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,
CC       RsxC, 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.
CC       RnfB subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
DR   EMBL; CP000243; ABE07296.1; -; Genomic_DNA.
DR   RefSeq; WP_000991809.1; NC_007946.1.
DR   ProteinModelPortal; Q1RBG8; -.
DR   SMR; Q1RBG8; -.
DR   EnsemblBacteria; ABE07296; ABE07296; UTI89_C1818.
DR   KEGG; eci:UTI89_C1818; -.
DR   HOGENOM; HOG000262938; -.
DR   KO; K03616; -.
DR   OMA; CIDMLPV; -.
DR   Proteomes; UP000001952; 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   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; Complete proteome;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Repeat; Translocase; Transport.
FT   CHAIN         1    192       Ion-translocating oxidoreductase complex
FT                                subunit B.
FT                                /FTId=PRO_1000013643.
FT   DOMAIN       32     91       4Fe-4S. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   DOMAIN      108    137       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   DOMAIN      138    167       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   REGION        1     26       Hydrophobic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   METAL        49     49       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        52     52       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        57     57       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        74     74       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       117    117       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       120    120       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       123    123       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       127    127       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       147    147       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       150    150       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       153    153       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       157    157       Iron-sulfur 2 (4Fe-4S).
FT                                {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
//
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