MSRB_SALHS
ID MSRB_SALHS Reviewed; 137 AA.
AC B4TGC8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=SeHA_C1418;
OS Salmonella heidelberg (strain SL476).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL476;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001120; ACF70238.1; -; Genomic_DNA.
DR RefSeq; WP_001519539.1; NC_011083.1.
DR AlphaFoldDB; B4TGC8; -.
DR SMR; B4TGC8; -.
DR KEGG; seh:SeHA_C1418; -.
DR HOGENOM; CLU_031040_8_5_6; -.
DR OMA; DEQWRAE; -.
DR Proteomes; UP000001866; Chromosome.
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; Zinc.
FT CHAIN 1..137
FT /note="Peptide methionine sulfoxide reductase MsrB"
FT /id="PRO_1000145381"
FT DOMAIN 7..129
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ SEQUENCE 137 AA; 15471 MW; 90F79ABD5B4283CF CRC64;
MANQPSAEEL KKKLSEMQFY VTQDRGTEPP FTGRLLHNKR DGVYHCLVCD TPLFHSHTKY
DSGCGWPSFY QPVSEEAIRY IDDFSHGMQR VEIRCGNCDA HLGHVFPDGP QPTGERYCVN
SASLAFSDEK NGDQLKG
