ID   B8ESF0_METSB            Unreviewed;       177 AA.
AC   B8ESF0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   10-JUN-2026, entry version 99.
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 {ECO:0000256|HAMAP-Rule:MF_01401};
GN   OrderedLocusNames=Msil_0870 {ECO:0000313|EMBL:ACK49840.1};
OS   Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS   13906 / BL2).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK49840.1, ECO:0000313|Proteomes:UP000002257};
RN   [1] {ECO:0000313|EMBL:ACK49840.1, ECO:0000313|Proteomes:UP000002257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2
RC   {ECO:0000313|Proteomes:UP000002257};
RX   PubMed=20472789; DOI=10.1128/JB.00506-10;
RA   Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA   Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT   "Complete genome sequence of the aerobic facultative methanotroph
RT   Methylocella silvestris BL2.";
RL   J. Bacteriol. 192:3840-3841(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001280; ACK49840.1; -; Genomic_DNA.
DR   RefSeq; WP_012589910.1; NC_011666.1.
DR   AlphaFoldDB; B8ESF0; -.
DR   STRING; 395965.Msil_0870; -.
DR   KEGG; msl:Msil_0870; -.
DR   eggNOG; COG0225; Bacteria.
DR   HOGENOM; CLU_031040_10_2_5; -.
DR   OrthoDB; 4174719at2; -.
DR   Proteomes; UP000002257; 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   FunFam; 3.30.1060.10:FF:000005; Peptide methionine sulfoxide reductase MsrA; 1.
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:UP000002257}.
FT   DOMAIN          6..158
FT                   /note="Peptide methionine sulphoxide reductase MsrA"
FT                   /evidence="ECO:0000259|Pfam:PF01625"
FT   ACT_SITE        14
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   177 AA;  19884 MW;  360632780974C313 CRC64;
     MTTQTERAVL AGGCFWGMQD LIRRYPGVIS TRVGYTGGDV PNATYRNHGT HAEAIEIIFD
     PEKISYRTLL EFFFQIHDPT TRNRQGNDVG LSYRSAIYYT SEEQKRVAAD AIADVDASGL
     WPGRVVTEVA PAGDFWEAEP EHQDYLERYP AGYTCHFIRP GWKLPVRAEA HKQSGAA
//