ID   MSRAB_TREPA             Reviewed;         291 AA.
AC   O83641;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Peptide methionine sulfoxide reductase msrB/msrA;
DE   Includes:
DE     RecName: Full=Peptide methionine sulfoxide reductase msrB;
DE              EC=1.8.4.12;
DE     AltName: Full=Peptide-methionine (R)-S-oxide reductase;
DE   Includes:
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=msrAB; Synonyms=msrA; OrderedLocusNames=TP_0633;
OS   Treponema pallidum.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA   Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA   Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA   Weidman J.F., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(1998).
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 (R)-S-oxide + thioredoxin.
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: In the N-terminal section; belongs to the msrB Met
CC       sulfoxide reductase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the msrA Met
CC       sulfoxide reductase family.
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DR   EMBL; AE000520; AAC65608.1; -; Genomic_DNA.
DR   PIR; G71300; G71300.
DR   RefSeq; NP_219071.1; -.
DR   HSSP; P14930; 1L1D.
DR   GeneID; 2611495; -.
DR   GenomeReviews; AE000520_GR; TP_0633.
DR   KEGG; tpa:TP0633; -.
DR   NMPDR; fig|243276.1.peg.630; -.
DR   TIGR; TP_0633; -.
DR   HOGENOM; O83641; -.
DR   OMA; O83641; GEQPYCQ.
DR   BioCyc; TPAL243276:TP_0633-MON; -.
DR   BRENDA; 1.8.4.11; 142600.
DR   BRENDA; 1.8.4.12; 142600.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase ac...; IEA:EC.
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_01400; fused; 1.
DR   HAMAP; MF_01401; fused; 1.
DR   InterPro; IPR002579; Methionine_sulphoxide_MsrB.
DR   InterPro; IPR002569; MsrA.
DR   Gene3D; G3DSA:3.30.1060.10; MsrA; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   Pfam; PF01641; SelR; 1.
DR   ProDom; PD004057; DUF25; 1.
DR   ProDom; PD003489; PMSR; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
DR   TIGRFAMs; TIGR00357; MsrB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Multifunctional enzyme; Oxidoreductase.
FT   CHAIN         1    291       Peptide methionine sulfoxide reductase
FT                                msrB/msrA.
FT                                /FTId=PRO_0000138525.
FT   REGION        1    124       Peptide methionine sulfoxide reductase B.
FT   REGION      127    284       Peptide methionine sulfoxide reductase A.
FT   ACT_SITE    113    113       By similarity.
FT   ACT_SITE    135    135       By similarity.
SQ   SEQUENCE   291 AA;  32802 MW;  3FF46CC8D37E8C15 CRC64;
     MLANLQHLSD IQYRVTQQSA TETPFKNEFW NSYQPGFYLD VVSGELLFLS EDKFDSGCGW
     PSFSAPAYAR AVIEKEDRTH NMLRTEVRSR NANSHLGHVF KDGPPERGGL RYCINSAALR
     FVAREEGTAL FAAGCFWSTE AYFRRVKGVL RVRVGYTGGT TKSPTYRNVC TGTTGHAEAV
     EILFDPQVIS YEDLLKHFFR MHDPTSLNKQ GGDVGTQYRS AIFYLSGTQK QQAETLMGRY
     AGAGKFTRPL VTTLEEARDF YPAEEYHQDY LTKNPGGYCH VSLHLASEPL E
//