ID   OGT_ECOLI               Reviewed;         171 AA.
AC   P0AFH0; P09168; P78284;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Methylated-DNA--protein-cysteine methyltransferase;
DE            EC=2.1.1.63;
DE   AltName: Full=6-O-methylguanine-DNA methyltransferase;
DE            Short=MGMT;
DE   AltName: Full=O-6-methylguanine-DNA-alkyltransferase;
GN   Name=ogt; OrderedLocusNames=b1335, JW1329;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=88067749; PubMed=2825131; DOI=10.1093/nar/15.22.9177;
RA   Potter P.M., Wilkinson M.C., Fitton J., Carr F.J., Brennand J.,
RA   Cooper D.P., Margison G.P.;
RT   "Characterisation and nucleotide sequence of ogt, the O6-alkylguanine-
RT   DNA-alkyltransferase gene of E. coli.";
RL   Nucleic Acids Res. 15:9177-9193(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97251357; PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   MUTAGENESIS OF CYSTEINE RESIDUES.
RX   MEDLINE=92392360; PubMed=1520330; DOI=10.1016/S0006-291X(05)81510-4;
RA   Harris L.C., Potter P.M., Margison G.P.;
RT   "Site directed mutagenesis of two cysteine residues in the E. coli ogt
RT   O6-alkylguanine DNA alkyltransferase protein.";
RL   Biochem. Biophys. Res. Commun. 187:425-431(1992).
CC   -!- FUNCTION: Involved in the cellular defense against the biological
CC       effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated
CC       guanine in DNA by stoichiometrically transferring the alkyl group
CC       at the O-6 position to a cysteine residue in the enzyme. This is a
CC       suicide reaction: the enzyme is irreversibly inactivated. Can also
CC       repair O-4-methylthymine.
CC   -!- CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein
CC       L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-
CC       cysteine.
CC   -!- SIMILARITY: Belongs to the MGMT family.
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DR   EMBL; Y00495; CAA68548.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74417.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14928.1; -; Genomic_DNA.
DR   PIR; B64883; XUECAD.
DR   RefSeq; AP_001963.1; -.
DR   RefSeq; NP_415851.1; -.
DR   HSSP; P16455; 1QNT.
DR   GeneID; 945853; -.
DR   GenomeReviews; AP009048_GR; JW1329.
DR   GenomeReviews; U00096_GR; b1335.
DR   KEGG; ecj:JW1329; -.
DR   KEGG; eco:b1335; -.
DR   EchoBASE; EB0662; -.
DR   EcoGene; EG10668; ogt.
DR   HOGENOM; P0AFH0; -.
DR   OMA; P0AFH0; WLLAHEN.
DR   BioCyc; EcoCyc:EG10668-MON; -.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methylt...; IEA:EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR   InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA_bd.
DR   InterPro; IPR008332; MethylG_MeTrfase.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR10815; MethylDNA_cys_mtrans_DNA_bd; 1.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   Pfam; PF02870; Methyltransf_1N; 1.
DR   TIGRFAMs; TIGR00589; ogt; 1.
DR   PROSITE; PS00374; MGMT; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; DNA damage; DNA repair;
KW   Methyltransferase; Transferase.
FT   CHAIN         1    171       Methylated-DNA--protein-cysteine
FT                                methyltransferase.
FT                                /FTId=PRO_0000139365.
FT   ACT_SITE    139    139       Nucleophile; methyl group acceptor
FT                                (Probable).
FT   MUTAGEN     102    102       C->G: Little effect on the activity.
FT   MUTAGEN     139    139       C->G: Eliminates the activity.
FT   CONFLICT     37     37       R -> A (in Ref. 1; CAA68548).
FT   CONFLICT     68     68       E -> D (in Ref. 1; CAA68548).
SQ   SEQUENCE   171 AA;  19179 MW;  39EFBF1539F67D26 CRC64;
     MLRLLEEKIA TPLGPLWVIC DEQFRLRAVE WEEYSERMVQ LLDIHYRKEG YERISATNPG
     GLSDKLREYF AGNLSIIDTL PTATGGTPFQ REVWKTLRTI PCGQVMHYGQ LAEQLGRPGA
     ARAVGAANGS NPISIVVPCH RVIGRNGTMT GYAGGVQRKE WLLRHEGYLL L
//