ID   Q5HPI0_STAEQ            Unreviewed;       171 AA.
AC   Q5HPI0;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   02-SEP-2026, entry version 127.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
GN   Name=msrA-1 {ECO:0000313|EMBL:AAW54321.1};
GN   Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401};
GN   OrderedLocusNames=SERP0931 {ECO:0000313|EMBL:AAW54321.1};
OS   Staphylococcus epidermidis (strain ATCC 35984 / DSM 28319 / BCRC 17069 /
OS   CCUG 31568 / BM 3577 / RP62A).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279 {ECO:0000313|EMBL:AAW54321.1, ECO:0000313|Proteomes:UP000000531};
RN   [1] {ECO:0000313|EMBL:AAW54321.1, ECO:0000313|Proteomes:UP000000531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A {ECO:0000313|Proteomes:UP000000531};
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., Deboy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L., Beanan M., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J., Khouri H., Utterback T., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K., Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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:0000256|ARBA:ARBA00024679, ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00047806, ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00048782, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000256|ARBA:ARBA00005591, ECO:0000256|HAMAP-Rule:MF_01401}.
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DR   EMBL; CP000029; AAW54321.1; -; Genomic_DNA.
DR   RefSeq; WP_002456531.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPI0; -.
DR   STRING; 176279.SERP0931; -.
DR   PaxDb; 176279-SERP0931; -.
DR   KEGG; ser:SERP0931; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_1_9; -.
DR   Proteomes; UP000000531; Chromosome.
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   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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01401}; Reference proteome {ECO:0000313|Proteomes:UP000000531}.
FT   DOMAIN          5..161
FT                   /note="Peptide methionine sulphoxide reductase MsrA"
FT                   /evidence="ECO:0000259|Pfam:PF01625"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   171 AA;  19862 MW;  BACEA45AE36CD83F CRC64;
     MNINTAYFAG GCFWCMTKPF DTFDGIEKVT SGYMGGHLVN PSYEEVKTGS TGHYEVVKIE
     YDVALFSYHK LLEIFFSVID PLDDGGQFQD RGSQYKTAIF YSNEHQRQLA EQYICELQDS
     FNADKAIATK ILPASTFYEA EVYHQDFYKK NPERYEQEQQ DRANYVKDNH M
//