(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 129.
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}.
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   SMR; P19220; -.
DR   STRING; 224308.BSU01820; -.
DR   PaxDb; P19220; -.
DR   PRIDE; P19220; -.
DR   EnsemblBacteria; CAB11958; CAB11958; BSU01820.
DR   GeneID; 938673; -.
DR   KEGG; bsu:BSU01820; -.
DR   PATRIC; fig|224308.179.peg.188; -.
DR   eggNOG; ENOG4105K85; Bacteria.
DR   eggNOG; COG0350; LUCA.
DR   HOGENOM; HOG000244137; -.
DR   InParanoid; P19220; -.
DR   KO; K13531; -.
DR   OMA; RFHIAAT; -.
DR   PhylomeDB; P19220; -.
DR   BioCyc; BSUB:BSU01820-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-EC.
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;
DR   PRODOM; P19220.
DR   SWISS-2DPAGE; P19220.
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
//

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