ID   MSRA1_CAUVC             Reviewed;         217 AA.
AC   Q9A9I6;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA 1;
DE            Short=Protein-methionine-S-oxide reductase 1;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase 1;
DE            Short=Peptide Met(O) reductase 1;
GN   Name=msrA1; OrderedLocusNames=CC_0994;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(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       (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; AE005673; AAK22978.1; -; Genomic_DNA.
DR   PIR; F87372; F87372.
DR   RefSeq; NP_419810.1; NC_002696.2.
DR   RefSeq; WP_010918878.1; NC_002696.2.
DR   AlphaFoldDB; Q9A9I6; -.
DR   SMR; Q9A9I6; -.
DR   STRING; 190650.CC_0994; -.
DR   EnsemblBacteria; AAK22978; AAK22978; CC_0994.
DR   KEGG; ccr:CC_0994; -.
DR   PATRIC; fig|190650.5.peg.1013; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_3_5; -.
DR   OMA; AGPFYYA; -.
DR   BioCyc; CAULO:CC0994-MON; -.
DR   Proteomes; UP000001816; 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; Reference proteome.
FT   CHAIN           1..217
FT                   /note="Peptide methionine sulfoxide reductase MsrA 1"
FT                   /id="PRO_0000138536"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  23044 MW;  ED945F0AA9FD933B CRC64;
     MLSLHKTLEM PSADTALPGR AAPIPTAQTH FVNGHALKGP YPEGLETAIV AMGCFWGVER
     VFWKVPGVYV TAAGYAAGIT PNPTYEEVCT GRTGHTEVVL VVFDPKVVTY EALLKTFWEN
     HDPTQGMRQG NDIGTQYRSG LYVTSDAQAA AAAESKAAYQ QALSARGLGT ITTEIAPAGP
     FYFAEDYHQQ YLAKNPNGYC GIGGTGVVCP IGLGVEG