ID MSRA1_STAA8 Reviewed; 169 AA. AC P0A084; Q2G2M1; Q99QD5; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 16-JUN-2009, entry version 24. 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=SAOUHSC_01360; OS Staphylococcus aureus (strain NCTC 8325). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Rossi J., Berger-Baechi B., Bischoff M.; RT "Identification of the mrsAR locus of Staphylococcus aureus BB270 RT involved in multiple resistance."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA Iandolo J.J.; RT "The Staphylococcus aureus NCTC8325 genome."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Has an important function as a repair enzyme for CC proteins that have been inactivated by oxidation. Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins CC to methionine (By similarity). CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. CC -!- SIMILARITY: Belongs to the msrA Met sulfoxide reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF311784; AAK00894.1; -; Genomic_DNA. DR EMBL; CP000253; ABD30455.1; -; Genomic_DNA. DR RefSeq; YP_499887.1; -. DR HSSP; P27110; 1FF3. DR GeneID; 3920065; -. DR GenomeReviews; CP000253_GR; SAOUHSC_01360. DR KEGG; sao:SAOUHSC_01360; -. DR HOGENOM; P0A084; -. DR OMA; P0A084; DDGGQFQ. DR BioCyc; SAUR93061:SAOUHSC_01360-MON; -. DR GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006464; P:protein modification process; IEA:HAMAP. DR HAMAP; MF_01401; -; 1. DR InterPro; IPR002569; MsrA. DR Gene3D; G3DSA:3.30.1060.10; MsrA; 1. DR Pfam; PF01625; PMSR; 1. DR ProDom; PD003489; PMSR; 1. DR TIGRFAMs; TIGR00401; msrA; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase. FT CHAIN 1 169 Peptide methionine sulfoxide reductase FT msrA 1. FT /FTId=PRO_0000138589. FT ACT_SITE 12 12 By similarity. 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 //