ID   MSRB_STAA8              Reviewed;         142 AA.
AC   P0A088; Q2FYK9; Q93P62;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=msrB; Synonyms=pilB; OrderedLocusNames=SAOUHSC_01431;
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   -!- 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         Evidence={ECO:0000269|PubMed:11700354, ECO:0000269|PubMed:11779133};
CC   -!- MISCELLANEOUS: Stereospecific for the R isomer of MetO.
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AF349112; AAK83252.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30523.1; -; Genomic_DNA.
DR   RefSeq; WP_000913315.1; NZ_LS483365.1.
DR   RefSeq; YP_499956.1; NC_007795.1.
DR   AlphaFoldDB; P0A088; -.
DR   SMR; P0A088; -.
DR   STRING; 1280.SAXN108_1444; -.
DR   EnsemblBacteria; ABD30523; ABD30523; SAOUHSC_01431.
DR   GeneID; 3920212; -.
DR   KEGG; sao:SAOUHSC_01431; -.
DR   PATRIC; fig|93061.5.peg.1307; -.
DR   eggNOG; COG0229; Bacteria.
DR   HOGENOM; CLU_031040_8_5_9; -.
DR   OMA; DEQWRAE; -.
DR   PHI-base; PHI:4582; -.
DR   PRO; PR:P0A088; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IBA:GO_Central.
DR   GO; GO:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   HAMAP; MF_01400; MsrB; 1.
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; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; SSF51316; 1.
DR   TIGRFAMs; TIGR00357; TIGR00357; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..142
FT                   /note="Peptide methionine sulfoxide reductase MsrB"
FT                   /id="PRO_0000140299"
FT   DOMAIN          2..125
FT                   /note="MsrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ   SEQUENCE   142 AA;  16277 MW;  8B8DD1390D9F80AD CRC64;
     MLKKDKSELT DIEYIVTQEN GTEPPFMNEY WNHFAKGIYV DKISGKPLFT SEEKFHSECG
     WPSFSKALDD DEIIELVDKS FGMLRTEVRS EESNSHLGHV FNDGPKESGG LRYCINSAAI
     QFIPYEKLEE LGYGDLISHF DK