ID A0A0R1LZT1_9LACO Unreviewed; 143 AA.
AC A0A0R1LZT1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=FC81_GL001338 {ECO:0000313|EMBL:KRL01197.1};
OS Liquorilactobacillus capillatus DSM 19910.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423731 {ECO:0000313|EMBL:KRL01197.1, ECO:0000313|Proteomes:UP000051621};
RN [1] {ECO:0000313|EMBL:KRL01197.1, ECO:0000313|Proteomes:UP000051621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19910 {ECO:0000313|EMBL:KRL01197.1,
RC ECO:0000313|Proteomes:UP000051621};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRL01197.1}.
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DR EMBL; AZEF01000027; KRL01197.1; -; Genomic_DNA.
DR RefSeq; WP_057744378.1; NZ_AZEF01000027.1.
DR AlphaFoldDB; A0A0R1LZT1; -.
DR STRING; 1423731.FC81_GL001338; -.
DR PATRIC; fig|1423731.3.peg.1376; -.
DR OrthoDB; 4174719at2; -.
DR Proteomes; UP000051621; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051621}.
FT DOMAIN 4..127
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ SEQUENCE 143 AA; 16123 MW; 6FDE828EDC103352 CRC64;
MESDKELKER LSKEEYEVTQ HAATEHPFSG KYDDFYQDGI YVDVVSGQAL FSSKDKYDAG
CGWPSFTQPI KKENITEHVD NSLLMTRTEV KSQEAASHLG HVFNDGPVDA GGMRYCINSA
ALKFIPVNKL EQAGYGEYRN LFD
//
