ID   MSRA_ACIBS              Reviewed;         174 AA.
AC   B0VL72;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   10-JUN-2026, entry version 96.
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};
GN   OrderedLocusNames=ABSDF3055;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Moraxellales; Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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=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; Evidence={ECO:0000255|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; 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; CU468230; CAP02340.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VL72; -.
DR   SMR; B0VL72; -.
DR   KEGG; abm:ABSDF3055; -.
DR   HOGENOM; CLU_031040_10_0_6; -.
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.
FT   CHAIN           1..174
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /id="PRO_1000145391"
FT   ACT_SITE        10
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   174 AA;  19962 MW;  54B5C18BFE9C4295 CRC64;
     MQQALFGGGC FWCVEAVFLQ IRGVEKVTSG YAGGHTTHPT YEQVCQGDTQ HAEVVLIDFD
     EQQVTYSQLL DVFFATHDPT TLNRQGNDIG TQYRSVIYYF NEEQKQAAEH TIQTLKDDDL
     DIVTELSPAP TFYPAEDYHQ NYYEKNPSQG YCNFAIPPKL LKLYSKFQHL MKDQ
//