ID   MSRA_BRUSU              Reviewed;         218 AA.
AC   Q8FUZ0;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Peptide methionine sulfoxide reductase msrA;
DE            Short=Protein-methionine-S-oxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
GN   Name=msrA; OrderedLocusNames=BRA1069;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
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.
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DR   EMBL; AE014292; AAN34236.1; -; Genomic_DNA.
DR   RefSeq; NP_700231.1; -.
DR   HSSP; P54149; 1FVA.
DR   GeneID; 1165515; -.
DR   GenomeReviews; AE014292_GR; BRA1069.
DR   KEGG; bms:BRA1069; -.
DR   NMPDR; fig|204722.1.peg.3140; -.
DR   TIGR; BRA1069; -.
DR   HOGENOM; Q8FUZ0; -.
DR   OMA; Q8FUZ0; YHQQYLD.
DR   BioCyc; BSUI204722:BR_A1069-MON; -.
DR   BRENDA; 1.8.4.11; 281610.
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    218       Peptide methionine sulfoxide reductase
FT                                msrA.
FT                                /FTId=PRO_0000138533.
FT   ACT_SITE     57     57       By similarity.
SQ   SEQUENCE   218 AA;  24075 MW;  64B7FE10667417B0 CRC64;
     MSFFDSYRKK MQMPSKEEVL PGRVQPIPTA AAHFVSGHPL KGPWPDGMKQ VLFGMGCFWG
     AERLFWQVPG VYVTAVGYAG GITPNPTYEE TCTGLTGHAE VVLVVYDPKV VTLNELLALF
     WEEHDPTQGM RQGNDIGTTY RSVIYTFNAV DRAVAEKSRD AYSQALASRG LGPVTTQIAD
     APDFYYAEDY HQQYLAKNPD GYCGLRGTDV SCPIPLAH
//