OGT_BACSU
ID OGT_BACSU Reviewed; 165 AA.
AC P11742;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase, constitutive {ECO:0000255|HAMAP-Rule:MF_00772};
DE EC=2.1.1.63 {ECO:0000255|HAMAP-Rule:MF_00772, ECO:0000269|PubMed:3100503};
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}; Synonyms=dat, dat1;
GN OrderedLocusNames=BSU13540;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2505068; DOI=10.1016/0921-8777(89)90022-0;
RA Kodama K., Nakabeppu Y., Sekiguchi M.;
RT "Cloning and expression of the Bacillus subtilis methyltransferase gene in
RT Escherichia coli ada- cells.";
RL Mutat. Res. 218:153-163(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=2506524; DOI=10.1093/nar/17.16.6531;
RA Morohoshi F., Hayashi K., Munakata N.;
RT "Bacillus subtilis gene coding for constitutive O6-methylguanine-DNA
RT alkyltransferase.";
RL Nucleic Acids Res. 17:6531-6543(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=168;
RX PubMed=3100503; DOI=10.1128/jb.169.2.587-592.1987;
RA Morohoshi F., Munakata N.;
RT "Multiple species of Bacillus subtilis DNA alkyltransferase involved in the
RT adaptive response to simple alkylating agents.";
RL J. Bacteriol. 169:587-592(1987).
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, ECO:0000269|PubMed:3100503}.
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 ECO:0000269|PubMed:3100503};
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 ECO:0000269|PubMed:3100503};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:3100503}.
CC -!- MISCELLANEOUS: Bacillus subtilis contains 2 species of O-6-
CC methylguanine-DNA alkyltransferases. Ogt and adaB are regulated in
CC different ways, constitutively and inducibly on adaptive treatment,
CC respectively.
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; X15659; CAA33694.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13227.1; -; Genomic_DNA.
DR PIR; S04877; XUBSM1.
DR RefSeq; NP_389237.1; NC_000964.3.
DR RefSeq; WP_003232502.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P11742; -.
DR SMR; P11742; -.
DR STRING; 224308.BSU13540; -.
DR PaxDb; P11742; -.
DR PRIDE; P11742; -.
DR EnsemblBacteria; CAB13227; CAB13227; BSU_13540.
DR GeneID; 939332; -.
DR KEGG; bsu:BSU13540; -.
DR PATRIC; fig|224308.179.peg.1470; -.
DR eggNOG; COG0350; Bacteria.
DR InParanoid; P11742; -.
DR OMA; QANRANE; -.
DR PhylomeDB; P11742; -.
DR BioCyc; BSUB:BSU13540-MON; -.
DR Proteomes; UP000001570; 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; 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; DNA damage; DNA repair; Methyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..165
FT /note="Methylated-DNA--protein-cysteine methyltransferase,
FT constitutive"
FT /id="PRO_0000139364"
FT ACT_SITE 130
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00772"
SQ SEQUENCE 165 AA; 18752 MW; 3B52393F34B5EE9F CRC64;
MNYYTTAETP LGELIIAEEE DRITRLFLSQ EDWVDWKETV QNTEHKETPN LAEAKQQLQE
YFAGERKTFS LPLSQKGTPF QQKVWQALER IPYGESRSYA DIAAAVGSPK AVRAVGQANK
RNDLPIFVPC HRVIGKNSAL TGYAGSKTEI KAFLLNIERI SYKEK
