MSRA2_LACLA
ID MSRA2_LACLA Reviewed; 172 AA.
AC Q9CE42;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA 2;
DE Short=Protein-methionine-S-oxide reductase 2;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase 2;
DE Short=Peptide Met(O) reductase 2;
GN Name=msrA2; Synonyms=pmsR; OrderedLocusNames=LL2006; ORFNames=L67708;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation. Catalyzes the reversible
CC oxidation-reduction of methionine sulfoxide in proteins to methionine
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:50058; EC=1.8.4.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58772; EC=1.8.4.11;
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AE005176; AAK06104.1; -; Genomic_DNA.
DR PIR; F86875; F86875.
DR RefSeq; NP_268163.1; NC_002662.1.
DR RefSeq; WP_010906260.1; NC_002662.1.
DR AlphaFoldDB; Q9CE42; -.
DR SMR; Q9CE42; -.
DR STRING; 272623.L67708; -.
DR PaxDb; Q9CE42; -.
DR EnsemblBacteria; AAK06104; AAK06104; L67708.
DR KEGG; lla:L67708; -.
DR PATRIC; fig|272623.7.peg.2161; -.
DR eggNOG; COG0225; Bacteria.
DR HOGENOM; CLU_031040_10_1_9; -.
DR OMA; PYIAYND; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..172
FT /note="Peptide methionine sulfoxide reductase MsrA 2"
FT /id="PRO_0000138552"
FT ACT_SITE 12
FT /evidence="ECO:0000250"
SQ SEQUENCE 172 AA; 19878 MW; B84CCD0C5FE7F06F CRC64;
MATERAIFAG GCFWCMVQPF EEREGILSVI SGYTGGNVEN PTYEQVKKHL TGHTEAVEII
FDNSKITYQS LVELYWTLTD PTDAFGQFED RGDNYRPVIF VENEEQEKIA KESKAQLQAS
GNFDSPIVTS IETVQKFWPA EDYHQGFYKK NPEDYAQSSK IRHDFLEKQW KK
