MSRA1_STAAM
ID MSRA1_STAAM Reviewed; 169 AA.
AC P0A081; Q99QD5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA 1;
DE Short=Protein-methionine-S-oxide reductase 1;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase 1;
DE Short=Peptide Met(O) reductase 1;
GN Name=msrA1; Synonyms=msrA; OrderedLocusNames=SAV1361;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP CATALYTIC ACTIVITY, AND STEREOSPECIFICITY.
RX PubMed=11779133; DOI=10.1006/bbrc.2001.6171;
RA Moskovitz J., Singh V.K., Requena J., Wilkinson B.J., Jayaswal R.K.,
RA Stadtman E.R.;
RT "Purification and characterization of methionine sulfoxide reductases from
RT mouse and Staphylococcus aureus and their substrate stereospecificity.";
RL Biochem. Biophys. Res. Commun. 290:62-65(2002).
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 Evidence={ECO:0000269|PubMed:11779133};
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 Evidence={ECO:0000269|PubMed:11779133};
CC -!- MISCELLANEOUS: Stereospecific for the S isomer of MetO.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; BA000017; BAB57523.1; -; Genomic_DNA.
DR RefSeq; WP_001024830.1; NC_002758.2.
DR AlphaFoldDB; P0A081; -.
DR SMR; P0A081; -.
DR World-2DPAGE; 0002:P0A081; -.
DR PaxDb; P0A081; -.
DR EnsemblBacteria; BAB57523; BAB57523; SAV1361.
DR KEGG; sav:SAV1361; -.
DR HOGENOM; CLU_031040_10_1_9; -.
DR OMA; GYCAFVV; -.
DR PhylomeDB; P0A081; -.
DR BioCyc; SAUR158878:SAV_RS07335-MON; -.
DR Proteomes; UP000002481; 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 1: Evidence at protein level;
KW Oxidoreductase.
FT CHAIN 1..169
FT /note="Peptide methionine sulfoxide reductase MsrA 1"
FT /id="PRO_0000138581"
FT ACT_SITE 12
FT /evidence="ECO:0000250"
SQ SEQUENCE 169 AA; 19611 MW; 6C5406148DAAC9A0 CRC64;
MNINTAYFAG GCFWCMTKPF DTFDGIEKVT SGYMGGHIEN PTYEQVKSGT SGHLETVEIQ
YDVALFSYNK LLEIFFSVID PLDTGGQYQD RGPQYQTAIF YTNDHQKELA ETYIEQLKNT
INADKAIATK ILPASQFYKA EDYHQDFYKK NPERYAEEQK IRQEYKNKQ
