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   03-AUG-2022, entry version 110.
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 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   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., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC   -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC       that have been inactivated by oxidation. Catalyzes the reversible
CC       oxidation-reduction of methionine sulfoxide in proteins to methionine
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC         ChEBI:CHEBI:50058; EC=1.8.4.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC         dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58772; EC=1.8.4.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC         ChEBI:CHEBI:50058; EC=1.8.4.12;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MsrA Met
CC       sulfoxide reductase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
CC       sulfoxide reductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL98136.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE009949; AAL98136.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8P046; -.
DR   SMR; Q8P046; -.
DR   KEGG; spm:spyM18_1571; -.
DR   HOGENOM; CLU_031040_1_1_9; -.
DR   GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   HAMAP; MF_01400; MsrB; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   PANTHER; PTHR10173; PTHR10173; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; SSF51316; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
DR   TIGRFAMs; TIGR00357; TIGR00357; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Multifunctional enzyme; Oxidoreductase.
FT   CHAIN           1..309
FT                   /note="Peptide methionine sulfoxide reductase MsrA/MsrB"
FT                   /id="PRO_0000138524"
FT   DOMAIN          170..293
FT                   /note="MsrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   REGION          1..153
FT                   /note="Peptide methionine sulfoxide reductase A"
FT   ACT_SITE        8
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        282
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
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