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MSRA2_STAA8
ID   MSRA2_STAA8             Reviewed;         177 AA.
AC   P0A086; Q2FYK8; Q93P63;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA 2;
DE            Short=Protein-methionine-S-oxide reductase 2;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase 2;
DE            Short=Peptide Met(O) reductase 2;
GN   Name=msrA2; Synonyms=msrA; OrderedLocusNames=SAOUHSC_01432;
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], AND CATALYTIC ACTIVITY.
RX   PubMed=11700354; DOI=10.1099/00221287-147-11-3037;
RA   Singh V.K., Moskovitz J., Wilkinson B.J., Jayaswal R.K.;
RT   "Molecular characterization of a chromosomal locus in Staphylococcus aureus
RT   that contributes to oxidative defence and is highly induced by the cell-
RT   wall-active antibiotic oxacillin.";
RL   Microbiology 147:3037-3045(2001).
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).
RN   [3]
RP   CATALYTIC ACTIVITY, AND STEREOSPECIFICITY.
RX   PubMed=11779133; DOI=10.1006/bbrc.2001.6171;
RA   Moskovitz J., Singh V.K., Requena J., Wilkinson B.J., Jayaswal R.K.,
RA   Stadtman E.R.;
RT   "Purification and characterization of methionine sulfoxide reductases from
RT   mouse and Staphylococcus aureus and their substrate stereospecificity.";
RL   Biochem. Biophys. Res. Commun. 290:62-65(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   -!- INDUCTION: Induced by oxacillin but not by hydrogen peroxide.
CC   -!- MISCELLANEOUS: Stereospecific for the S isomer of MetO.
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AF349112; AAK83251.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30524.1; -; Genomic_DNA.
DR   RefSeq; WP_000159902.1; NZ_LS483365.1.
DR   RefSeq; YP_499957.1; NC_007795.1.
DR   AlphaFoldDB; P0A086; -.
DR   SMR; P0A086; -.
DR   STRING; 1280.SAXN108_1445; -.
DR   EnsemblBacteria; ABD30524; ABD30524; SAOUHSC_01432.
DR   GeneID; 3920213; -.
DR   KEGG; sao:SAOUHSC_01432; -.
DR   PATRIC; fig|93061.5.peg.1308; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_1_9; -.
DR   OMA; AGPFYYA; -.
DR   PHI-base; PHI:4580; -.
DR   PRO; PR:P0A086; -.
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   1: Evidence at protein level;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..177
FT                   /note="Peptide methionine sulfoxide reductase MsrA 2"
FT                   /id="PRO_0000138590"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   177 AA;  20588 MW;  6BE5ABDE1545A5D4 CRC64;
     MTKEYATLAG GCFWCMVKPF TSYPGIKSVV SGYSGGHVDN PTYEQVCTNQ TGHVEAVQIT
     FDPEVTSFEN ILDIYFKTFD PTDDQGQFFD RGESYQPVIF YHDEHQKKAA EFKKQQLNEQ
     GIFKKPVITP IKPYKNFYPA EDYHQDYYKK NPVHYYQYQR GSGRKAFIES HWGNQNA
 
 
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