ID   Q8FPI7_COREF            Unreviewed;       137 AA.
AC   Q8FPI7; C8NP98;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   04-NOV-2026, entry version 128.
DE   RecName: Full=peptide-methionine (R)-S-oxide reductase {ECO:0000256|ARBA:ARBA00012499};
DE            EC=1.8.4.12 {ECO:0000256|ARBA:ARBA00012499};
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18601.1, ECO:0000313|Proteomes:UP000001409};
RN   [1] {ECO:0000313|EMBL:BAC18601.1, ECO:0000313|Proteomes:UP000001409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC   {ECO:0000313|Proteomes:UP000001409};
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L-
CC         methionyl-(R)-S-oxide-[protein] + [thioredoxin]-dithiol;
CC         Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC         ChEBI:CHEBI:50058; EC=1.8.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00048488};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01126}.
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DR   EMBL; BA000035; BAC18601.1; -; Genomic_DNA.
DR   RefSeq; WP_006767789.1; NC_004369.1.
DR   AlphaFoldDB; Q8FPI7; -.
DR   STRING; 196164.gene:10742219; -.
DR   KEGG; cef:CE1791; -.
DR   eggNOG; COG0229; Bacteria.
DR   HOGENOM; CLU_031040_8_5_11; -.
DR   OMA; AAEHNMA; -.
DR   OrthoDB; 9785497at2; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR   FunFam; 2.170.150.20:FF:000009; Peptide-methionine (R)-S-oxide reductase; 1.
DR   Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR   InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR   PANTHER; PTHR10173; METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR10173:SF52; METHIONINE-R-SULFOXIDE REDUCTASE B1; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01126};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|PROSITE-
KW   ProRule:PRU01126}; Reference proteome {ECO:0000313|Proteomes:UP000001409};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01126}.
FT   DOMAIN          9..133
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
FT   ACT_SITE        122
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01126"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01126"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01126"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01126"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01126"
SQ   SEQUENCE   137 AA;  15643 MW;  C4175F5714A297AF CRC64;
     MTDFKLITDA EWRERLNPEE YRVLRQAGTE APHVGEYTNT TTEGVYSCRA CGEELFRSTE
     KFDAHCGWPS FFSPLAKDKI IEKEDLSLGM RRIEVLCANC GSHMGHVFEG EGFNTPTDLR
     YCINSISLRL EEKPVSE
//