ID A0P6W7_9PROT Unreviewed; 241 AA.
AC A0P6W7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=MB2181_04350 {ECO:0000313|EMBL:EAV47277.1};
OS Methylophilales bacterium HTCC2181.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OM43 clade.
OX NCBI_TaxID=383631 {ECO:0000313|EMBL:EAV47277.1, ECO:0000313|Proteomes:UP000054262};
RN [1] {ECO:0000313|EMBL:EAV47277.1, ECO:0000313|Proteomes:UP000054262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2181 {ECO:0000313|EMBL:EAV47277.1,
RC ECO:0000313|Proteomes:UP000054262};
RA Giovannoni S., Vergin K., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (NOV-2006) 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:EAV47277.1}.
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DR EMBL; AAUX01000001; EAV47277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0P6W7; -.
DR OrthoDB; 4174719at2; -.
DR Proteomes; UP000054262; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.40.30.10; Glutaredoxin; 1.
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 InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
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 Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51790; MSRB; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000054262}.
FT DOMAIN 124..241
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
SQ SEQUENCE 241 AA; 26774 MW; E52C28412830DB61 CRC64;
MKKLLVSTEH FLAFLVLFIC SLTTIAGDKR LNDLTDVLNG EDLANQQLVV FESETCGSCK
AFNKDILTGW KSALNIKKTY SMQAPSGWEL KEDLWATPTI LFFEDGKEVS RYTGYDGNKQ
AFWQWLGLQT LTPEQKKIAF ESGTERAFTG SLLDNHAPGF YVDPISGEQL FRSDNKFNSG
TGWPSFFNPV PGSIVYKDDG HRVEVLSASS GIHLGHVFND GPPPTGKRYC INSAVLKFVA
D
//
