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Database: UniProt
Entry: A0A0T2KWR4_9MICO
LinkDB: A0A0T2KWR4_9MICO
Original site: A0A0T2KWR4_9MICO 
ID   A0A0T2KWR4_9MICO        Unreviewed;       159 AA.
AC   A0A0T2KWR4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=peptide-methionine (R)-S-oxide reductase {ECO:0000256|ARBA:ARBA00012499};
DE            EC=1.8.4.12 {ECO:0000256|ARBA:ARBA00012499};
GN   ORFNames=ASD65_06400 {ECO:0000313|EMBL:KRA24094.1};
OS   Microbacterium sp. Root61.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA24094.1, ECO:0000313|Proteomes:UP000051216};
RN   [1] {ECO:0000313|EMBL:KRA24094.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA24094.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA24094.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA24094.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRA24094.1}.
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DR   EMBL; LMGU01000001; KRA24094.1; -; Genomic_DNA.
DR   RefSeq; WP_056220032.1; NZ_LMGU01000001.1.
DR   AlphaFoldDB; A0A0T2KWR4; -.
DR   STRING; 1736570.ASD65_06400; -.
DR   OrthoDB; 9785497at2; -.
DR   Proteomes; UP000051216; Unassembled WGS sequence.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC.
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   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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051216}.
FT   DOMAIN          8..131
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
SQ   SEQUENCE   159 AA;  17839 MW;  4EC4A5B5236D9FC8 CRC64;
     MSHDYRKTPE AIERLTPQQF HVTQEQGTEP AFRNEYWNNH EPGLYVDVVS GQPLFSSTDK
     YDSGTGWPSF TRPLARDAVT EHVDGMLWMK RTEVRSSSVG SHLGHVFDDG PRDAGGMRYC
     MNSASLRFIP AADLEAQGYG EYRELFDGAA DTTTQENAS
//
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