ID   MSRB_BURVG              Reviewed;         143 AA.
AC   A4JEZ1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Bcep1808_1841;
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01400};
CC       Note=Binds 1 zinc ion per subunit. The zinc ion is important for the
CC       structural integrity of the protein. {ECO:0000255|HAMAP-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; CP000614; ABO54844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4JEZ1; -.
DR   SMR; A4JEZ1; -.
DR   STRING; 269482.Bcep1808_1841; -.
DR   EnsemblBacteria; ABO54844; ABO54844; Bcep1808_1841.
DR   KEGG; bvi:Bcep1808_1841; -.
DR   eggNOG; COG0229; Bacteria.
DR   HOGENOM; CLU_031040_8_5_4; -.
DR   OMA; DEQWRAE; -.
DR   Proteomes; UP000002287; Chromosome 1.
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: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   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..143
FT                   /note="Peptide methionine sulfoxide reductase MsrB"
FT                   /id="PRO_1000145363"
FT   DOMAIN          16..139
FT                   /note="MsrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   ACT_SITE        128
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ   SEQUENCE   143 AA;  16239 MW;  018E97A409CFBC23 CRC64;
     MSHDSDDKTY PYQKDDAELR RRLTPMQYEV TQHAATERAF TGEYTDTEDA GIYKCVVCST
     PLFESGAKFH SGCGWPSYFK PLNGEVIDEK IDRSHGMVRV EVRCNHCGAH LGHVFEDGPR
     DQTGLRYCIN SAALNFESRP ENE