ID   MSRB_LACLA              Reviewed;         142 AA.
AC   Q9CJ17;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000255|HAMAP-Rule:MF_01400};
DE            EC=1.8.4.12 {ECO:0000255|HAMAP-Rule:MF_01400};
DE   AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01400};
GN   Name=msrB {ECO:0000255|HAMAP-Rule:MF_01400}; Synonyms=ybjA;
GN   OrderedLocusNames=LL0189; ORFNames=L192996;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01400};
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01400}.
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DR   EMBL; AE005176; AAK04287.1; -; Genomic_DNA.
DR   PIR; E86648; E86648.
DR   RefSeq; NP_266345.1; NC_002662.1.
DR   RefSeq; WP_010905188.1; NC_002662.1.
DR   AlphaFoldDB; Q9CJ17; -.
DR   SMR; Q9CJ17; -.
DR   STRING; 272623.L192996; -.
DR   PaxDb; Q9CJ17; -.
DR   PRIDE; Q9CJ17; -.
DR   EnsemblBacteria; AAK04287; AAK04287; L192996.
DR   KEGG; lla:L192996; -.
DR   PATRIC; fig|272623.7.peg.210; -.
DR   eggNOG; COG0229; Bacteria.
DR   HOGENOM; CLU_031040_8_5_9; -.
DR   OMA; DEQWRAE; -.
DR   Proteomes; UP000002196; Chromosome.
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   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   PANTHER; PTHR10173; PTHR10173; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; SSF51316; 1.
DR   TIGRFAMs; TIGR00357; TIGR00357; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..142
FT                   /note="Peptide methionine sulfoxide reductase MsrB"
FT                   /id="PRO_0000140276"
FT   DOMAIN          3..126
FT                   /note="MsrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ   SEQUENCE   142 AA;  16144 MW;  D93C104C1CBA7026 CRC64;
     MEKEKLKKKL SLLAYRVTQE NGTEAPFANE FDDFFEQGLY VDVVSGEALF TSLDKYQSGC
     GWPAFTQPID KGVVKEKRDK SLFMERTEVR SSNADSHLGH VFTDGPLDKG DLRYCINSAA
     LRFVPFDQLE AEGYGEYVKY FS