ID   MSRB_PSE14              Reviewed;         131 AA.
AC   Q48FR2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=PSPPH_3630;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ35748.1; -; Genomic_DNA.
DR   RefSeq; YP_275773.1; -.
DR   GeneID; 3558347; -.
DR   GenomeReviews; CP000058_GR; PSPPH_3630.
DR   KEGG; psp:PSPPH_3630; -.
DR   NMPDR; fig|264730.3.peg.3787; -.
DR   HOGENOM; Q48FR2; -.
DR   OMA; Q48FR2; FTGRYWD.
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   CHAIN         1    131       Peptide methionine sulfoxide reductase
FT                                msrB.
FT                                /FTId=PRO_1000068281.
FT   ACT_SITE    119    119       Nucleophile (By similarity).
FT   METAL        47     47       Zinc (By similarity).
FT   METAL        50     50       Zinc (By similarity).
FT   METAL        96     96       Zinc (By similarity).
FT   METAL        99     99       Zinc (By similarity).
SQ   SEQUENCE   131 AA;  14719 MW;  48637D134EFB1E05 CRC64;
     MDKLQKTLEE WKEMLDPAQY QVCRLKGTER PFSGKYNETK TEGVYHCICC NEPLFDSTTK
     FDSGCGWPSF YAPLEGSAVV EVRDVSHGMI RTEVVCAKCD AHLGHVFPDG PPPTGLRYCI
     NSVCLDLVPR Q
//