ID   MSRAB_STRP8             Reviewed;         309 AA.
AC   Q8P046;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 2.
DT   24-MAR-2009, entry version 42.
DE   RecName: Full=Peptide methionine sulfoxide reductase msrA/msrB;
DE   Includes:
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;
DE   Includes:
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=msrAB; OrderedLocusNames=spyM18_1571;
OS   Streptococcus pyogenes serotype M18.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232 / Serotype M18;
RX   MEDLINE=21927593; PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F.,
RA   Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q.,
RA   Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18
RT   group A Streptococcus strains associated with acute rheumatic fever
RT   outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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   -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
CC       H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the msrA Met
CC       sulfoxide reductase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the msrB Met
CC       sulfoxide reductase family.
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DR   EMBL; AE009949; AAL98136.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_607637.1; -.
DR   HSSP; P14930; 1L1D.
DR   GeneID; 994664; -.
DR   GenomeReviews; AE009949_GR; spyM18_1571.
DR   KEGG; spm:spyM18_1571; -.
DR   HOGENOM; Q8P046; -.
DR   BioCyc; SPYO186103:SPYM18_1571-MON; -.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006464; P:protein modification process; IEA:HAMAP.
DR   HAMAP; MF_01400; fused; 1.
DR   HAMAP; MF_01401; fused; 1.
DR   InterPro; IPR002579; Methionine_sulphoxide_MsrB.
DR   InterPro; IPR002569; MsrA.
DR   Gene3D; G3DSA:3.30.1060.10; MsrA; 1.
DR   Gene3D; G3DSA:2.170.150.20; MsrB; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   Pfam; PF01641; SelR; 1.
DR   ProDom; PD004057; DUF25; 1.
DR   ProDom; PD003489; PMSR; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
DR   TIGRFAMs; TIGR00357; MsrB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Multifunctional enzyme; Oxidoreductase.
FT   CHAIN         1    309       Peptide methionine sulfoxide reductase
FT                                msrA/msrB.
FT                                /FTId=PRO_0000138524.
FT   REGION        1    153       Peptide methionine sulfoxide reductase A.
FT   REGION      170    293       Peptide methionine sulfoxide reductase B.
FT   ACT_SITE      8      8       By similarity.
FT   ACT_SITE    282    282       By similarity.
SQ   SEQUENCE   309 AA;  35133 MW;  2E1F1374F4028ADF CRC64;
     MIYLAGGCFW GVEEYFSQVD GVLDAVSGYA NGRGDTTNYQ LIHQTGHAET VEVAYDTNRI
     SLKELLLHFF RIIDPTSLNK QGNDRGSQYR TGIYYTDKAD LAIIDEVFKE KAKDYKKKIV
     VEKAPLKHFI KAEDYHQDYL KKNPNGYCHI DINQATYPVI DESKYPKPSA TEIKEKLSAD
     EYRVTQKNET EKAFSNRYWD SFDAGIYVDV VTGEPLFSSK DKFESGCGWP SFSRPISPDV
     VRYKEDKSFN MTRTEVRSRS GNSHLGHVFT DGPKDQGGLR YCINSLSITF IPKADMEAKG
     YGYLLSSVE
//