MSRB_STAHJ
ID MSRB_STAHJ Reviewed; 142 AA.
AC Q4L6D3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 120.
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}; OrderedLocusNames=SH1483;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04792.1; -; Genomic_DNA.
DR RefSeq; WP_011275778.1; NC_007168.1.
DR AlphaFoldDB; Q4L6D3; -.
DR SMR; Q4L6D3; -.
DR STRING; 279808.SH1483; -.
DR EnsemblBacteria; BAE04792; BAE04792; SH1483.
DR GeneID; 58062314; -.
DR KEGG; sha:SH1483; -.
DR eggNOG; COG0229; Bacteria.
DR HOGENOM; CLU_031040_8_5_9; -.
DR OMA; DEQWRAE; -.
DR OrthoDB; 1650261at2; -.
DR Proteomes; UP000000543; 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.
FT CHAIN 1..142
FT /note="Peptide methionine sulfoxide reductase MsrB"
FT /id="PRO_0000140303"
FT DOMAIN 2..125
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ SEQUENCE 142 AA; 16377 MW; 2138EB898A8E43A7 CRC64;
MIKKDKNELN EMEYLVTQEN GTEPPFQNEY WNHFDKGIYV DKISGKPLFT SEEKFESNCG
WPSFSKSIDD DEIIELVDKT FGMIRTEVRS EDANSHLGHV FNDGPKESGG LRYCINSAAI
QFIPYDKLEE LGYGDLIPHF EK