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Database: UniProt
Entry: A0A1V1PQC5_9PROT
LinkDB: A0A1V1PQC5_9PROT
Original site: A0A1V1PQC5_9PROT 
ID   A0A1V1PQC5_9PROT        Unreviewed;       177 AA.
AC   A0A1V1PQC5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=U91I_02286 {ECO:0000313|EMBL:GAM98651.1};
OS   alpha proteobacterium U9-1i.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1605283 {ECO:0000313|EMBL:GAM98651.1, ECO:0000313|Proteomes:UP000188260};
RN   [1] {ECO:0000313|EMBL:GAM98651.1, ECO:0000313|Proteomes:UP000188260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U9-1i {ECO:0000313|EMBL:GAM98651.1,
RC   ECO:0000313|Proteomes:UP000188260};
RA   Okano K., Furuta S., Ichise S., Miyata N.;
RT   "Whole-Genome Sequences of Two Manganese(II)-Oxidizing Bacteria, Bosea sp.
RT   Strain BIWAKO-01 and Alphaproteobacterium Strain U9-1i.";
RL   Genome Announc. 4:e01309-16(2016).
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:GAM98651.1}.
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DR   EMBL; BBSY01000002; GAM98651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1PQC5; -.
DR   STRING; 1605283.U91I_02286; -.
DR   OrthoDB; 9785497at2; -.
DR   Proteomes; UP000188260; 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   ECO:0000313|EMBL:GAM98651.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188260};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..177
FT                   /note="peptide-methionine (R)-S-oxide reductase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010722113"
FT   DOMAIN          28..153
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
SQ   SEQUENCE   177 AA;  19263 MW;  5C2A0EFA121C303D CRC64;
     MKPLPLIIAG TVAALVAGAA LFLSQPRDAS ANAESRFEAL RTYVMDFGGT ERAFDNEYWD
     HHEPGIYVEA RTGEPLFAST DKFDSGSGWP SFTRPIDVSA VAAREDSSAG MTRVEIRSKQ
     GDAHLGHVFN DGPRERGGQR YCINSCAIRF IPRAEMEAQG YGAYTHLIDN PQPAPAS
//
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