ID   MSRB_HATHI              Reviewed;         159 AA.
AC   Q9ZNJ9;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 88.
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};
OS   Hathewaya histolytica (Clostridium histolyticum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hathewaya.
OX   NCBI_TaxID=1498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19401 / DSM 2158 / JCM 1403 / NCIMB 503 / NCTC 503;
RX   PubMed=9922257; DOI=10.1128/jb.181.3.923-933.1999;
RA   Matsushita O., Jung C.-M., Katayama S., Minami J., Takahashi Y., Okabe A.;
RT   "Gene duplication and multiplicity of collagenases in Clostridium
RT   histolyticum.";
RL   J. Bacteriol. 181:923-933(1999).
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; AB014075; BAA34541.1; -; Genomic_DNA.
DR   PIR; T44354; T44354.
DR   AlphaFoldDB; Q9ZNJ9; -.
DR   SMR; Q9ZNJ9; -.
DR   OrthoDB; 4174719at2; -.
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   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 B3; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..159
FT                   /note="Peptide methionine sulfoxide reductase MsrB"
FT                   /id="PRO_0000140268"
FT   DOMAIN          14..137
FT                   /note="MsrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ   SEQUENCE   159 AA;  18531 MW;  FF50ACEEA1871231 CRC64;
     MNHKKEKEYK KLDTEKLKEN LTELQYNVTQ RNATEKPFLN KYDKHFEDGI YVDIVSGEPL
     FLSIDKFNSG CGWPAFSKPI SRKYIKERAD FSHGMSRIEV RSKNADSHLG HVFNDGPIEN
     GGMRYCINSA SLKFIAKDKL KEEGYEEFLP LFEKDKQEL
//