ADAB_BACSU
ID ADAB_BACSU Reviewed; 179 AA.
AC P19220;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase, inducible;
DE EC=2.1.1.63 {ECO:0000269|PubMed:3100503};
DE AltName: Full=O-6-methylguanine-DNA alkyltransferase;
DE AltName: Full=O6-methylguanine-DNA methyltransferase;
DE Short=MGMT;
GN Name=adaB; OrderedLocusNames=BSU01820;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ROLE IN RESISTANCE TO
RP ALKYLATION DAMAGE, AND INDUCTION.
RC STRAIN=168;
RX PubMed=2120677; DOI=10.1093/nar/18.18.5473;
RA Morohoshi F., Hayashi K., Munakata N.;
RT "Bacillus subtilis ada operon encodes two DNA alkyltransferases.";
RL Nucleic Acids Res. 18:5473-5480(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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, AND CATALYTIC ACTIVITY.
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).
RN [5]
RP MUTAGENESIS.
RX PubMed=1744039; DOI=10.1128/jb.173.24.7834-7840.1991;
RA Morohoshi F., Hayashi K., Munakata N.;
RT "Molecular analysis of Bacillus subtilis ada mutants deficient in the
RT adaptive response to simple alkylating agents.";
RL J. Bacteriol. 173:7834-7840(1991).
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:0000269|PubMed:2120677, 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|PROSITE-ProRule:PRU10017,
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|PROSITE-ProRule:PRU10017,
CC ECO:0000269|PubMed:3100503};
CC -!- INDUCTION: Up-regulated by methylated AdaA in response to the exposure
CC to alkylating agents such as MNNG. {ECO:0000269|PubMed:2120677}.
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:0000305}.
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; X53399; CAA37476.1; -; Genomic_DNA.
DR EMBL; AB006424; BAA33075.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11958.1; -; Genomic_DNA.
DR PIR; S11564; XUBSMB.
DR RefSeq; NP_388063.1; NC_000964.3.
DR RefSeq; WP_003246311.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P19220; -.
DR SMR; P19220; -.
DR STRING; 224308.BSU01820; -.
DR PaxDb; P19220; -.
DR EnsemblBacteria; CAB11958; CAB11958; BSU_01820.
DR GeneID; 938673; -.
DR KEGG; bsu:BSU01820; -.
DR PATRIC; fig|224308.179.peg.188; -.
DR eggNOG; COG0350; Bacteria.
DR InParanoid; P19220; -.
DR OMA; RFHIAAT; -.
DR PhylomeDB; P19220; -.
DR BioCyc; BSUB:BSU01820-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006304; P:DNA modification; IEA:UniProt.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd06445; ATase; 1.
DR Gene3D; 1.10.10.10; -; 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; 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 DNA damage; DNA repair; Methyltransferase; Reference proteome; Transferase.
FT CHAIN 1..179
FT /note="Methylated-DNA--protein-cysteine methyltransferase,
FT inducible"
FT /id="PRO_0000139374"
FT ACT_SITE 141
FT /note="Nucleophile; methyl group acceptor"
FT MUTAGEN 141
FT /note="C->Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1744039"
FT MUTAGEN 167
FT /note="L->P: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1744039"
SQ SEQUENCE 179 AA; 20124 MW; BC30C65C6B76B64A CRC64;
METNKPTLYW SLLMFKDWNF YIASTLKGLV FVGSQNKPIE ELFEWARKRF PGSLLVEDDD
KLEPYAVEIT QYLEGKRKNF TVPVEYAGTQ FQLAVWNALC EIPYGQTKSY SDIANDINKP
AAVRAVGAAI GANPVLITVP CHRVIGKNGS LTGYRGGFEM KTLLLDLEKR ASSEMDVPH
