ID MSRB_ECOL6 Reviewed; 137 AA. AC P0A747; P39903; P76232; P76912; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 1. DT 16-JUN-2009, entry version 29. DE RecName: Full=Peptide methionine sulfoxide reductase msrB; DE EC=1.8.4.12; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase; GN Name=msrB; OrderedLocusNames=c2183; OS Escherichia coli O6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=217992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC; RX MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC -!- COFACTOR: Binds 1 zinc ion per subunit. The zinc ion is important CC for the structural integrity of the protein (By similarity). CC -!- SIMILARITY: Belongs to the msrB Met sulfoxide reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014075; AAN80642.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_754077.1; -. DR HSSP; P14930; 1L1D. DR GeneID; 1036623; -. DR GenomeReviews; AE014075_GR; c2183. DR KEGG; ecc:c2183; -. DR HOGENOM; P0A747; -. DR OMA; P0A747; FTGRYWD. DR BRENDA; 1.8.4.12; 292881. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase ac...; IEA:EC. DR GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01400; -; 1. DR InterPro; IPR002579; Methionine_sulphoxide_MsrB. DR Gene3D; G3DSA:2.170.150.20; MsrB; 1. DR Pfam; PF01641; SelR; 1. DR ProDom; PD004057; DUF25; 1. DR TIGRFAMs; TIGR00357; MsrB; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Oxidoreductase; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 137 Peptide methionine sulfoxide reductase FT msrB. FT /FTId=PRO_0000140273. FT ACT_SITE 118 118 Nucleophile (By similarity). FT METAL 46 46 Zinc (By similarity). FT METAL 49 49 Zinc (By similarity). FT METAL 95 95 Zinc (By similarity). FT METAL 98 98 Zinc (By similarity). SQ SEQUENCE 137 AA; 15451 MW; 7B9B783DBEBE0F71 CRC64; MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD APLFHSQTKY DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA HLGHVFPDGP QPTGERYCVN SASLRFTDGE NGEEING //