ID   MSRA_LISIN              Reviewed;         177 AA.
AC   Q92AE8;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000255|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase {ECO:0000255|HAMAP-Rule:MF_01401};
GN   Name=msrA {ECO:0000255|HAMAP-Rule:MF_01401}; OrderedLocusNames=lin1974;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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:0000255|HAMAP-Rule:MF_01401}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01401}.
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DR   EMBL; AL596170; CAC97204.1; -; Genomic_DNA.
DR   PIR; AD1679; AD1679.
DR   RefSeq; WP_003769341.1; NC_003212.1.
DR   AlphaFoldDB; Q92AE8; -.
DR   SMR; Q92AE8; -.
DR   STRING; 272626.lin1974; -.
DR   EnsemblBacteria; CAC97204; CAC97204; CAC97204.
DR   GeneID; 61171539; -.
DR   KEGG; lin:lin1974; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_1_9; -.
DR   OMA; PYIAYND; -.
DR   OrthoDB; 1554384at2; -.
DR   Proteomes; UP000002513; 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   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..177
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /id="PRO_0000138553"
FT   ACT_SITE        15
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   177 AA;  19933 MW;  6B422E15AFAFCF91 CRC64;
     MTKESLEKAT FAGGCFWCMV KPFDTQPGIE KVVSGYTGGH TVNPTYKEVC SGTTGHTEAV
     EITFDPAVFP YEKLVEVYWQ QTDPTDAAGQ FVDRGDSYRP VIFYHNEEQR QIAEKSKAAL
     DASGRFKKPV VTEIAKAETF YPAEEYHQDF YKKEKAHYEG YQVASGRAAF IDANWKG