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Database: UniProt
Entry: A0A0B0I653_9BACI
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ID   A0A0B0I653_9BACI        Unreviewed;       176 AA.
AC   A0A0B0I653;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
DE            EC=2.1.1.63 {ECO:0000256|HAMAP-Rule:MF_00772};
DE   AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
DE            Short=MGMT {ECO:0000256|HAMAP-Rule:MF_00772};
DE   AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
GN   ORFNames=LQ50_24700 {ECO:0000313|EMBL:KHF37908.1};
OS   Halalkalibacter okhensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF37908.1, ECO:0000313|Proteomes:UP000030832};
RN   [1] {ECO:0000313|EMBL:KHF37908.1, ECO:0000313|Proteomes:UP000030832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA   Prakash J.S.;
RT   "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001286,
CC         ECO:0000256|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:0000256|ARBA:ARBA00001596, ECO:0000256|HAMAP-
CC         Rule:MF_00772};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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       {ECO:0000256|HAMAP-Rule:MF_00772}.
CC   -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000256|HAMAP-
CC       Rule:MF_00772}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHF37908.1}.
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DR   EMBL; JRJU01000063; KHF37908.1; -; Genomic_DNA.
DR   RefSeq; WP_034634003.1; NZ_JRJU01000063.1.
DR   AlphaFoldDB; A0A0B0I653; -.
DR   STRING; 333138.LQ50_24700; -.
DR   eggNOG; COG0350; Bacteria.
DR   OrthoDB; 9802228at2; -.
DR   Proteomes; UP000030832; Unassembled WGS sequence.
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; 3.30.160.70; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   NCBIfam; TIGR00589; ogt; 1.
DR   PANTHER; PTHR10815; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10815:SF5; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   Pfam; PF02870; Methyltransf_1N; 1.
DR   SUPFAM; SSF53155; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR   SUPFAM; SSF46767; Methylated DNA-protein cysteine methyltransferase, C-terminal domain; 1.
DR   PROSITE; PS00374; MGMT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00772};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00772};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00772};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00772}; Reference proteome {ECO:0000313|Proteomes:UP000030832};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00772}.
FT   DOMAIN          12..87
FT                   /note="Methylguanine DNA methyltransferase ribonuclease-
FT                   like"
FT                   /evidence="ECO:0000259|Pfam:PF02870"
FT   DOMAIN          91..171
FT                   /note="Methylated-DNA-[protein]-cysteine S-
FT                   methyltransferase DNA binding"
FT                   /evidence="ECO:0000259|Pfam:PF01035"
FT   ACT_SITE        142
FT                   /note="Nucleophile; methyl group acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00772"
SQ   SEQUENCE   176 AA;  19488 MW;  56966748A50601DD CRC64;
     MTTQLIHYVD EMNSPLGTLT IVATEKGVCH IHFGELTKCS VSLKAWLKKQ GRKGEVIRCK
     ETLQPICEQL EDYFAGKRDR FDVPLDLCGT EFQKKVWNTL QEIEYGQTKS YKEIAQQIGA
     PKAVRAIGGA NNQNPVPIII PCHRVIGSNG NMVGYGGGLD KKELLLSLEG AIEKIS
//
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