ID   MSRA_CLOBH              Reviewed;         157 AA.
AC   A5I348; A7G4K8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 15.
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=CBO1923, CLC_1868;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J.,
RA   Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T.,
RA   Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N.,
RA   Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E.,
RA   Sanders M., Simmonds M., White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum
RT   strain Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-
RT   A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000727; ABS38947.1; -; Genomic_DNA.
DR   EMBL; AM412317; CAL83465.1; -; Genomic_DNA.
DR   RefSeq; YP_001254426.1; -.
DR   RefSeq; YP_001387723.1; -.
DR   GeneID; 5186178; -.
DR   GeneID; 5399299; -.
DR   GenomeReviews; AM412317_GR; CBO1923.
DR   GenomeReviews; CP000727_GR; CLC_1868.
DR   KEGG; cbh:CLC_1868; -.
DR   KEGG; cbo:CBO1923; -.
DR   OMA; A5I348; PFYFAED.
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    157       Peptide methionine sulfoxide reductase
FT                                msrA.
FT                                /FTId=PRO_1000068319.
FT   ACT_SITE     10     10       By similarity.
SQ   SEQUENCE   157 AA;  18178 MW;  E4458E31DD3FC694 CRC64;
     MKEIVLAGGC FWGVEEYMSR IEGIVETKVG YANGIKENPS YEEVCSGVTG HAEACYIKYD
     ESIISLEELL NKFWSIIDPT VLNKQGNDRG TQYRTGIFYL DEKDLNVIIK SKYQEQKNYR
     KPIVTEVEPL KCFYEAEEYH QKYLKKNPGG YCHIHLD
//