OGT_ECOLI
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 03-AUG-2022, entry version 119.
DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
DE EC=2.1.1.63 {ECO:0000255|HAMAP-Rule:MF_00772};
DE AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
DE Short=MGMT {ECO:0000255|HAMAP-Rule:MF_00772};
DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
GN Name=ogt {ECO:0000255|HAMAP-Rule:MF_00772};
GN OrderedLocusNames=b1335, JW1329;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX 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-DNA-
RT 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 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., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP MUTAGENESIS OF CYSTEINE RESIDUES.
RX 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 O6-
RT 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) and O4-methylthymine (O4-MeT) in
CC DNA. Repairs the methylated nucleobase in DNA by stoichiometrically
CC transferring the methyl group to a cysteine residue in the enzyme. This
CC is a suicide reaction: the enzyme is irreversibly inactivated.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein]
CC = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a
CC thymidine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:53428, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, ChEBI:CHEBI:137387;
CC EC=2.1.1.63; Evidence={ECO:0000255|HAMAP-Rule:MF_00772};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772}.
CC -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and therefore is
CC not strictly catalytic. According to one definition, an enzyme is a
CC biocatalyst that acts repeatedly and over many reaction cycles.
CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000255|HAMAP-
CC Rule:MF_00772}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; NP_415851.1; NC_000913.3.
DR RefSeq; WP_000945011.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P0AFH0; -.
DR SMR; P0AFH0; -.
DR BioGRID; 4262876; 110.
DR DIP; DIP-48073N; -.
DR IntAct; P0AFH0; 6.
DR STRING; 511145.b1335; -.
DR jPOST; P0AFH0; -.
DR PaxDb; P0AFH0; -.
DR PRIDE; P0AFH0; -.
DR EnsemblBacteria; AAC74417; AAC74417; b1335.
DR EnsemblBacteria; BAA14928; BAA14928; BAA14928.
DR GeneID; 58391829; -.
DR GeneID; 945853; -.
DR KEGG; ecj:JW1329; -.
DR KEGG; eco:b1335; -.
DR PATRIC; fig|1411691.4.peg.942; -.
DR EchoBASE; EB0662; -.
DR eggNOG; COG0350; Bacteria.
DR HOGENOM; CLU_000445_52_2_6; -.
DR InParanoid; P0AFH0; -.
DR OMA; SACAMNA; -.
DR PhylomeDB; P0AFH0; -.
DR BioCyc; EcoCyc:EG10668-MON; -.
DR BioCyc; MetaCyc:EG10668-MON; -.
DR PRO; PR:P0AFH0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:EcoCyc.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd06445; ATase; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00772; OGT; 1.
DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR InterPro; IPR008332; MethylG_MeTrfase_N.
DR InterPro; IPR023546; MGMT.
DR InterPro; IPR036631; MGMT_N_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01035; DNA_binding_1; 1.
DR Pfam; PF02870; Methyltransf_1N; 1.
DR SUPFAM; SSF46767; SSF46767; 1.
DR SUPFAM; SSF53155; SSF53155; 1.
DR TIGRFAMs; TIGR00589; ogt; 1.
DR PROSITE; PS00374; MGMT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
KW Methyltransferase; Reference proteome; Transferase.
FT CHAIN 1..171
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139365"
FT ACT_SITE 139
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000305"
FT MUTAGEN 102
FT /note="C->G: Little effect on the activity."
FT /evidence="ECO:0000269|PubMed:1520330"
FT MUTAGEN 139
FT /note="C->G: Eliminates the activity."
FT /evidence="ECO:0000269|PubMed:1520330"
FT CONFLICT 37
FT /note="R -> A (in Ref. 1; CAA68548)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> D (in Ref. 1; CAA68548)"
FT /evidence="ECO:0000305"
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
