ID   Q04DR3_OENOB            Unreviewed;       141 AA.
AC   Q04DR3;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   02-SEP-2026, entry version 106.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000256|HAMAP-Rule:MF_01400};
DE            EC=1.8.4.12 {ECO:0000256|HAMAP-Rule:MF_01400};
DE   AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01400};
GN   Name=msrB {ECO:0000256|HAMAP-Rule:MF_01400};
GN   OrderedLocusNames=OEOE_1554 {ECO:0000313|EMBL:ABJ57409.1};
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ57409.1, ECO:0000313|Proteomes:UP000000774};
RN   [1] {ECO:0000313|EMBL:ABJ57409.1, ECO:0000313|Proteomes:UP000000774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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, ECO:0000256|HAMAP-
CC         Rule:MF_01400};
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01400, ECO:0000256|PROSITE-
CC       ProRule:PRU01126}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01400,
CC       ECO:0000256|PROSITE-ProRule:PRU01126}.
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DR   EMBL; CP000411; ABJ57409.1; -; Genomic_DNA.
DR   RefSeq; WP_002817626.1; NC_008528.1.
DR   AlphaFoldDB; Q04DR3; -.
DR   STRING; 203123.OEOE_1554; -.
DR   GeneID; 75066464; -.
DR   KEGG; ooe:OEOE_1554; -.
DR   eggNOG; COG0229; Bacteria.
DR   HOGENOM; CLU_031040_8_5_9; -.
DR   Proteomes; UP000000774; 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:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   FunFam; 2.170.150.20:FF:000003; Peptide methionine sulfoxide reductase MsrB; 1.
DR   Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR   HAMAP; MF_01400; MsrB; 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:SF59; PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA_MSRB; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01400}; Reference proteome {ECO:0000313|Proteomes:UP000000774}.
FT   DOMAIN          2..125
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400,
FT                   ECO:0000256|PROSITE-ProRule:PRU01126"
SQ   SEQUENCE   141 AA;  15717 MW;  F710346215F2E86A CRC64;
     MADKDLSHLS KEQYEVTQKG ATERAFTGKY DDFYEEGIYV DVVDGTPLFS SKDKYDAGCG
     WPSFTKPIEN PSIVKKIDQS LGMTRTEVRS KDSGSHLGHV FDDGPDDKGG LRYCINSAAL
     KFIPVKELKK AGYGEYLSLF K
//