ID   MSRB_PSEA8              Reviewed;         132 AA.
AC   B7UUZ9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=PLES_22381;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(2009).
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; FM209186; CAW26965.1; -; Genomic_DNA.
DR   RefSeq; WP_003090911.1; NC_011770.1.
DR   AlphaFoldDB; B7UUZ9; -.
DR   SMR; B7UUZ9; -.
DR   KEGG; pag:PLES_22381; -.
DR   HOGENOM; CLU_031040_8_5_6; -.
DR   OMA; DEQWRAE; -.
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..132
FT                   /note="Peptide methionine sulfoxide reductase MsrB"
FT                   /id="PRO_1000145377"
FT   DOMAIN          8..130
FT                   /note="MsrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   ACT_SITE        119
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ   SEQUENCE   132 AA;  14825 MW;  640E0AEBEBFC055A CRC64;
     MSKIDKPLDS WREELTEEQF HICRLGGTER AFSGEYHATK TPGIYHCTCC GTALFDSDAK
     YDSGSGWPSY FQPVDAEAVR ELDDFSHGMH RIEVRCGRCD AHLGHVFPDG PRPTGLRYCI
     NSASLKLVPR ES