ID MSRB_SALTI Reviewed; 137 AA. AC P65450; Q8XGD3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 10-JUN-2026, entry version 121. 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=STY1824, t1170; OS Salmonella typhi. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., RA Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella enterica RT serovar Typhi CT18."; RL Nature 413:848-852(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., RA Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and RT CT18."; RL J. Bacteriol. 185:2330-2337(2003). 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO68827.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAD02063.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL513382; CAD02063.1; ALT_INIT; Genomic_DNA. DR EMBL; AE014613; AAO68827.1; ALT_INIT; Genomic_DNA. DR PIR; AF0711; AF0711. DR RefSeq; WP_001519539.1; NZ_CALNVT020000001.1. DR AlphaFoldDB; P65450; -. DR SMR; P65450; -. DR STRING; 220341.gene:17585755; -. DR KEGG; stt:t1170; -. DR KEGG; sty:STY1824; -. DR PATRIC; fig|220341.7.peg.1836; -. DR eggNOG; COG0229; Bacteria. DR HOGENOM; CLU_031040_8_5_6; -. DR OMA; YDETTDW; -. DR Proteomes; UP000002670; 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: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 FunFam; 2.170.150.20:FF:000001; 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:SF52; METHIONINE-R-SULFOXIDE REDUCTASE B1; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; Mss4-like; 1. DR PROSITE; PS51790; MSRB; 1. PE 3: Inferred from homology; KW Metal-binding; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1..137 FT /note="Peptide methionine sulfoxide reductase MsrB" FT /id="PRO_0000140293" 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 //