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Database: UniProt
Entry: A0A0E9MYC5_9BACT
LinkDB: A0A0E9MYC5_9BACT
Original site: A0A0E9MYC5_9BACT 
ID   A0A0E9MYC5_9BACT        Unreviewed;       178 AA.
AC   A0A0E9MYC5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=peptide-methionine (R)-S-oxide reductase {ECO:0000256|ARBA:ARBA00012499};
DE            EC=1.8.4.12 {ECO:0000256|ARBA:ARBA00012499};
GN   Name=msrB {ECO:0000313|EMBL:GAO42411.1};
GN   ORFNames=FPE01S_01_14260 {ECO:0000313|EMBL:GAO42411.1};
OS   Flavihumibacter petaseus NBRC 106054.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavihumibacter.
OX   NCBI_TaxID=1220578 {ECO:0000313|EMBL:GAO42411.1, ECO:0000313|Proteomes:UP000033121};
RN   [1] {ECO:0000313|EMBL:GAO42411.1, ECO:0000313|Proteomes:UP000033121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106054 {ECO:0000313|EMBL:GAO42411.1,
RC   ECO:0000313|Proteomes:UP000033121};
RA   Miyazawa S., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K., Ohji S.,
RA   Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT   "Whole genome shotgun sequence of Flavihumibacter petaseus NBRC 106054.";
RL   Submitted (APR-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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:GAO42411.1}.
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DR   EMBL; BBWV01000001; GAO42411.1; -; Genomic_DNA.
DR   RefSeq; WP_046368110.1; NZ_BBWV01000001.1.
DR   AlphaFoldDB; A0A0E9MYC5; -.
DR   STRING; 1220578.FPE01S_01_14260; -.
DR   Proteomes; UP000033121; 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 B1; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033121};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..178
FT                   /note="peptide-methionine (R)-S-oxide reductase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002429992"
FT   DOMAIN          53..175
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
SQ   SEQUENCE   178 AA;  20109 MW;  6DB889E1334CDAD3 CRC64;
     MTLSRIILFV CLAMLQQCSF SQPSPKKSTN MADTTKKNPL YSHEATDKVT LSDEEWKKVL
     PADVYYIARQ KGTERPWTSP FENSKEIGTY YCKACGNALF KSDTKFESGC GWPSFYEPVS
     KGSIIYTPDN SHGMRRTEVQ CGRCKAHLGH VFEDGPPPTG LRYCINGVIL DFEKTKEK
//
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