ID   MSRA2_STAAN             Reviewed;         177 AA.
AC   P65446; Q99U63;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
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; OrderedLocusNames=SA1257;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42517.1; -; Genomic_DNA.
DR   PIR; H89919; H89919.
DR   RefSeq; WP_000159900.1; NC_002745.2.
DR   AlphaFoldDB; P65446; -.
DR   SMR; P65446; -.
DR   EnsemblBacteria; BAB42517; BAB42517; BAB42517.
DR   KEGG; sau:SA1257; -.
DR   HOGENOM; CLU_031040_10_1_9; -.
DR   OMA; AGPFYYA; -.
DR   Proteomes; UP000000751; Chromosome.
DR   GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
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.
FT   CHAIN           1..177
FT                   /note="Peptide methionine sulfoxide reductase MsrA 2"
FT                   /id="PRO_0000138584"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   177 AA;  20588 MW;  E9F04BDE155045DB CRC64;
     MTKEYATLAG GCFWCMVKPF TSYPGIKSVV SGYSGGHVDN PTYEQVCTNK TGHVEAVQIT
     FDPEVTSFEN ILDIYFKTFD PTDDQGQFFD RGESYQPVIF YHDEHQKKAA EFKKQQLNEQ
     GIFKKPVITP IKPYKNFYPA EDYHQDYYKK NPVHYYQYQR GSGRKAFIES HWGNQNA