ID A0A1H9NYP0_9BACI Unreviewed; 141 AA.
AC A0A1H9NYP0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000256|HAMAP-Rule:MF_01400};
DE EC=1.8.4.12 {ECO:0000256|HAMAP-Rule:MF_01400};
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01400};
GN Name=msrB {ECO:0000256|HAMAP-Rule:MF_01400};
GN ORFNames=SAMN05518684_10169 {ECO:0000313|EMBL:SER41106.1};
OS Salipaludibacillus aurantiacus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=1601833 {ECO:0000313|EMBL:SER41106.1, ECO:0000313|Proteomes:UP000198571};
RN [1] {ECO:0000313|EMBL:SER41106.1, ECO:0000313|Proteomes:UP000198571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S9 {ECO:0000313|EMBL:SER41106.1,
RC ECO:0000313|Proteomes:UP000198571};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001795, ECO:0000256|HAMAP-
CC Rule:MF_01400};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000256|HAMAP-Rule:MF_01400}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01400}.
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DR EMBL; FOGT01000001; SER41106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9NYP0; -.
DR STRING; 1601833.SAMN05518684_10169; -.
DR OrthoDB; 4174719at2; -.
DR Proteomes; UP000198571; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01400}.
FT DOMAIN 3..125
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ SEQUENCE 141 AA; 15902 MW; 4D8F2CB88B5E431A CRC64;
MNKEDLKNKL TPIQYKVTQE DGTEPPFKNP LWDFFEEGLY VDVVSGEPLF SSNDKFESSC
GWPSFTKPLK SDAVVEKKDT SHFMIRTEVR SAEADSHLGH VFTDGPKPGG LRYCINSASL
RFIPADQLEE EGYGGFKSIF K
//
