ID   MSRA_VIBCH              Reviewed;         212 AA.
AC   Q9KP30;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA;
DE            Short=Protein-methionine-S-oxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
GN   Name=msrA; OrderedLocusNames=VC_2549;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF95690.1; -; Genomic_DNA.
DR   PIR; E82061; E82061.
DR   RefSeq; NP_232177.1; NC_002505.1.
DR   RefSeq; WP_000884809.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KP30; -.
DR   SMR; Q9KP30; -.
DR   STRING; 243277.VC_2549; -.
DR   DNASU; 2615566; -.
DR   EnsemblBacteria; AAF95690; AAF95690; VC_2549.
DR   GeneID; 57741152; -.
DR   KEGG; vch:VC_2549; -.
DR   PATRIC; fig|243277.26.peg.2427; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_3_6; -.
DR   OMA; AGPFYYA; -.
DR   BioCyc; VCHO:VC2549-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
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   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..212
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /id="PRO_0000138607"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  23360 MW;  AD50686E8BF13016 CRC64;
     MLDKQTMVTA HNALPGRTTA MSIDDTHFVN GSSLTAAPQS GQQQILIGMG CFWGAERLFW
     QLDGVISTSV GYSGGFTPNP TYEEVCSGKT GHTEVVRVIF DPERLPLTEL LRAFWERHDP
     TQGMRQGNDR GTQYRSAIYT FSEDQREIAE ASKAAYQALL TAQHRPSITT EILPAGAYYF
     AETYHQQYLA KNPNGYCGLG GTGVCFPPHS TL