ID   MSRB_LIGS1              Reviewed;         144 AA.
AC   Q1WVT3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   28-JAN-2026, entry version 101.
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};
GN   OrderedLocusNames=LSL_0029;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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; 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; CP000233; ABD98852.1; -; Genomic_DNA.
DR   RefSeq; WP_011475469.1; NC_007929.1.
DR   AlphaFoldDB; Q1WVT3; -.
DR   SMR; Q1WVT3; -.
DR   STRING; 362948.LSL_0029; -.
DR   KEGG; lsl:LSL_0029; -.
DR   PATRIC; fig|362948.14.peg.103; -.
DR   HOGENOM; CLU_031040_8_5_9; -.
DR   OrthoDB; 4174719at2; -.
DR   Proteomes; UP000006559; 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; Reference proteome.
FT   CHAIN           1..144
FT                   /note="Peptide methionine sulfoxide reductase MsrB"
FT                   /id="PRO_1000068276"
FT   DOMAIN          5..128
FT                   /note="MsrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   ACT_SITE        117
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ   SEQUENCE   144 AA;  16452 MW;  2EDC7614E42CD591 CRC64;
     MKETKEELRQ RIGEEAYQVT QNAATERAFT GKYDEFFEDG IYVDVVSGEP LFSSKDKYNS
     GCGWPAFTQP INNRMVTNHE DNSFGMHRVE VRSRQAQSHL GHVFNDGPQD RGGLRYCINS
     AALQFIPVAE LDEKGYGEYK KLFD
//