MSRB_HATHI
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 25-MAY-2022, entry version 83.
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; Firmicutes; 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 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..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