ID   MSRA1_STAAR             Reviewed;         169 AA.
AC   Q6GH44;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   04-NOV-2026, entry version 114.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA 1 {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase 1 {ECO:0000255|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000255|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase 1 {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase 1 {ECO:0000255|HAMAP-Rule:MF_01401};
GN   Name=msrA1 {ECO:0000255|HAMAP-Rule:MF_01401};
GN   OrderedLocusNames=SAR1373;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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       {ECO:0000255|HAMAP-Rule:MF_01401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L-
CC         methionyl-(S)-S-oxide-[protein] + [thioredoxin]-dithiol;
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + L-methionine + H2O = L-methionine
CC         (S)-S-oxide + [thioredoxin]-dithiol; 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01401}.
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DR   EMBL; BX571856; CAG40371.1; -; Genomic_DNA.
DR   RefSeq; WP_001024830.1; NC_002952.2.
DR   AlphaFoldDB; Q6GH44; -.
DR   SMR; Q6GH44; -.
DR   KEGG; sar:SAR1373; -.
DR   HOGENOM; CLU_031040_10_1_9; -.
DR   OMA; AAEPYHQ; -.
DR   GO; GO:0033744; F:L-methionine (S)-S-oxide reductase activity; IEA:RHEA.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   FunFam; 3.30.1060.10:FF:000003; Peptide methionine sulfoxide reductase MsrA; 1.
DR   Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   NCBIfam; TIGR00401; msrA; 1.
DR   PANTHER; PTHR43774; PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR43774:SF1; PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA 2; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..169
FT                   /note="Peptide methionine sulfoxide reductase MsrA 1"
FT                   /id="PRO_0000138585"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   169 AA;  19611 MW;  6C5406148DAAC9A0 CRC64;
     MNINTAYFAG GCFWCMTKPF DTFDGIEKVT SGYMGGHIEN PTYEQVKSGT SGHLETVEIQ
     YDVALFSYNK LLEIFFSVID PLDTGGQYQD RGPQYQTAIF YTNDHQKELA ETYIEQLKNT
     INADKAIATK ILPASQFYKA EDYHQDFYKK NPERYAEEQK IRQEYKNKQ
//