ID   MSRA_CLAM3              Reviewed;         175 AA.
AC   A5CQY7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 11.
DE   RecName: Full=Peptide methionine sulfoxide reductase msrA;
DE            Short=Protein-methionine-S-oxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
GN   Name=msrA; OrderedLocusNames=CMM_1446;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O.,
RA   Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S.,
RA   Rueckert C., Schneiker S., Zellermann E.-M., Puehler A.,
RA   Eichenlaub R., Kaiser O., Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island
RT   involved in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
CC   -!- FUNCTION: Has an important function as a repair enzyme for
CC       proteins that have been inactivated by oxidation. Catalyzes the
CC       reversible oxidation-reduction of methionine sulfoxide in proteins
CC       to methionine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
CC       H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
CC   -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
CC       L-methionine (S)-S-oxide + thioredoxin.
CC   -!- SIMILARITY: Belongs to the msrA Met sulfoxide reductase family.
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DR   EMBL; AM711867; CAN01491.1; -; Genomic_DNA.
DR   RefSeq; YP_001222187.1; -.
DR   GeneID; 5174695; -.
DR   GenomeReviews; AM711867_GR; CMM_1446.
DR   KEGG; cmi:CMM_1446; -.
DR   OMA; A5CQY7; QYRSAMF.
DR   GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006464; P:protein modification process; IEA:HAMAP.
DR   HAMAP; MF_01401; -; 1.
DR   InterPro; IPR002569; MsrA.
DR   Gene3D; G3DSA:3.30.1060.10; MsrA; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   ProDom; PD003489; PMSR; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Oxidoreductase.
FT   CHAIN         1    175       Peptide methionine sulfoxide reductase
FT                                msrA.
FT                                /FTId=PRO_1000068317.
FT   ACT_SITE     10     10       By similarity.
SQ   SEQUENCE   175 AA;  19172 MW;  3DF4D0B25B2D338B CRC64;
     MQTFILAGGC FWCLDAVYRT LDGVQDVISG YIGGHTAHPS YDAVCTGATG HAEAVKVVFD
     EEVIPADVIL DVFFTLHDPR QLNRQGADVG TQYRSAMFPA DAAQEQLFRD AISRAGELWD
     GTAVTTIEPV GTWYDAEDYH QDFFAKNPGQ GYCNAVAVPK VNKVRKSFAQ YVRAA
//