ID   MSRA1_STAA8             Reviewed;         169 AA.
AC   P0A084; Q2G2M1; Q99QD5;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA 1;
DE            Short=Protein-methionine-S-oxide reductase 1;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase 1;
DE            Short=Peptide Met(O) reductase 1;
GN   Name=msrA1; Synonyms=msrA; OrderedLocusNames=SAOUHSC_01360;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Rossi J., Berger-Baechi B., Bischoff M.;
RT   "Identification of the mrsAR locus of Staphylococcus aureus BB270 involved
RT   in multiple resistance.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AF311784; AAK00894.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30455.1; -; Genomic_DNA.
DR   RefSeq; WP_001024830.1; NZ_LS483365.1.
DR   RefSeq; YP_499887.1; NC_007795.1.
DR   AlphaFoldDB; P0A084; -.
DR   SMR; P0A084; -.
DR   STRING; 1280.SAXN108_1377; -.
DR   EnsemblBacteria; ABD30455; ABD30455; SAOUHSC_01360.
DR   GeneID; 3920065; -.
DR   KEGG; sao:SAOUHSC_01360; -.
DR   PATRIC; fig|93061.5.peg.1244; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_1_9; -.
DR   OMA; GYCAFVV; -.
DR   PRO; PR:P0A084; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..169
FT                   /note="Peptide methionine sulfoxide reductase MsrA 1"
FT                   /id="PRO_0000138589"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000250"
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