ID   OGT_SULIK               Reviewed;         151 AA.
AC   C4KKV8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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}; OrderedLocusNames=M164_0289;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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       {ECO:0000255|HAMAP-Rule:MF_00772}.
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}.
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DR   EMBL; CP001402; ACR40923.1; -; Genomic_DNA.
DR   RefSeq; WP_010923891.1; NC_012726.1.
DR   AlphaFoldDB; C4KKV8; -.
DR   SMR; C4KKV8; -.
DR   EnsemblBacteria; ACR40923; ACR40923; M164_0289.
DR   GeneID; 7808242; -.
DR   GeneID; 7940155; -.
DR   GeneID; 8760125; -.
DR   KEGG; sid:M164_0289; -.
DR   HOGENOM; CLU_000445_52_2_2; -.
DR   OMA; QANRANE; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:UniProtKB-UniRule.
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; IPR023546; MGMT.
DR   InterPro; IPR036631; MGMT_N_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   SUPFAM; SSF46767; SSF46767; 1.
DR   SUPFAM; SSF53155; SSF53155; 1.
DR   TIGRFAMs; TIGR00589; ogt; 1.
DR   PROSITE; PS00374; MGMT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Methyltransferase; Transferase.
FT   CHAIN           1..151
FT                   /note="Methylated-DNA--protein-cysteine methyltransferase"
FT                   /id="PRO_1000212902"
FT   ACT_SITE        119
FT                   /note="Nucleophile; methyl group acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00772"
SQ   SEQUENCE   151 AA;  17037 MW;  8457864CD5BC8F99 CRC64;
     MLVYGLYKSP LGYITVAKDD KGFIMLDFCD CVEGNSRDDS SFTEFFHKLD LYFEGKPINL
     REPINLKTYP FRLSVFKEVM KIPWGKVMTY KQIADSLGTS PRAVGMALSK NPILLIIPCH
     RVIAENGIGG YSRGVKLKRA LLELEGVKIP E