(data stored in ACNUC7421 zone)

SWISSPROT: ADAA_BACSU

ID   ADAA_BACSU              Reviewed;         211 AA.
AC   P19219;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   11-DEC-2019, entry version 146.
DE   RecName: Full=Bifunctional transcriptional activator/DNA repair enzyme AdaA;
DE   AltName: Full=Methylphosphotriester-DNA methyltransferase;
DE   AltName: Full=Methylphosphotriester-DNA--protein-cysteine S-methyltransferase;
DE            EC=2.1.1.n11;
GN   Name=adaA; OrderedLocusNames=BSU01810;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR,
RP   ROLE IN RESISTANCE TO 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   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).
RN   [6]
RP   FUNCTION.
RC   STRAIN=168;
RX   PubMed=8376346; DOI=10.1128/jb.175.18.6010-6017.1993;
RA   Morohoshi F., Hayashi K., Munakata N.;
RT   "Bacillus subtilis alkA gene encoding inducible 3-methyladenine DNA
RT   glycosylase is adjacent to the ada operon.";
RL   J. Bacteriol. 175:6010-6017(1993).
CC   -!- FUNCTION: Is involved in the adaptive response to alkylation damage in
CC       DNA caused by alkylating agents. Repairs the methylphosphotriester
CC       lesions in DNA by a direct and irreversible transfer of the methyl
CC       group to one of its own cysteine residues.
CC   -!- FUNCTION: The methylation of AdaA by methylphosphotriesters in DNA
CC       leads to its activation as a transcriptional regulator that activates
CC       the transcription of the ada operon which consists of adaA and adaB,
CC       and of the adjacent gene alkA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a methylphosphotriester deoxyribonucleoside in DNA + L-
CC         cysteinyl-[protein] = a deoxyribonucleotide in DNA + H(+) + S-methyl-
CC         L-cysteinyl-[protein]; Xref=Rhea:RHEA:56324, Rhea:RHEA-COMP:10131,
CC         Rhea:RHEA-COMP:10132, Rhea:RHEA-COMP:14462, Rhea:RHEA-COMP:14463,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:82612,
CC         ChEBI:CHEBI:140284, ChEBI:CHEBI:140286; EC=2.1.1.n11;
CC         Evidence={ECO:0000269|PubMed:3100503};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- INDUCTION: Up-regulated by methylated AdaA itself in response to the
CC       exposure to alkylating agents such as MNNG.
CC       {ECO:0000269|PubMed:2120677}.
DR   EMBL; X53399; CAA37475.1; -; Genomic_DNA.
DR   EMBL; AB006424; BAA33074.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11957.1; -; Genomic_DNA.
DR   PIR; S11483; XUBSMM.
DR   RefSeq; NP_388062.1; NC_000964.3.
DR   RefSeq; WP_003234924.1; NZ_JNCM01000030.1.
DR   SMR; P19219; -.
DR   STRING; 224308.BSU01810; -.
DR   PaxDb; P19219; -.
DR   PRIDE; P19219; -.
DR   EnsemblBacteria; CAB11957; CAB11957; BSU01810.
DR   GeneID; 938648; -.
DR   KEGG; bsu:BSU01810; -.
DR   PATRIC; fig|224308.179.peg.187; -.
DR   eggNOG; COG2169; LUCA.
DR   HOGENOM; HOG000062743; -.
DR   InParanoid; P19219; -.
DR   KO; K13530; -.
DR   OMA; PYHLQRT; -.
DR   PhylomeDB; P19219; -.
DR   BioCyc; BSUB:BSU01810-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.10.10; -; 1.
DR   InterPro; IPR035451; Ada-like_dom_sf.
DR   InterPro; IPR004026; Ada_DNA_repair_Zn-bd.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR016220; Me-P-triester_DNA_alkyl-Trfase.
DR   Pfam; PF02805; Ada_Zn_binding; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   PIRSF; PIRSF000408; Alkyltransferas_AdaA; 1.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   SUPFAM; SSF57884; SSF57884; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P19219.
DR   SWISS-2DPAGE; P19219.
KW   Activator; DNA damage; DNA repair; DNA-binding; Metal-binding;
KW   Methyltransferase; Reference proteome; Transcription;
KW   Transcription regulation; Transferase; Zinc.
FT   CHAIN           1..211
FT                   /note="Bifunctional transcriptional activator/DNA repair
FT                   enzyme AdaA"
FT                   /id="PRO_0000194494"
FT   DOMAIN          102..200
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   DNA_BIND        119..140
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   ACT_SITE        54
FT                   /note="Nucleophile; methyl group acceptor from
FT                   methylphosphotriester"
FT                   /evidence="ECO:0000250"
FT   METAL           54
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           58
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           85
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           88
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         86..87
FT                   /note="KR->NC: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1744039"
SQ   SEQUENCE   211 AA;  24299 MW;  920931082527EC27 CRC64;
     MPDSINNGHK ESHDHRISND AEMITDEKWQ AIINNDAAYN NQFFYAVKST GIFCKPSCKS
     RVPKKENVCI FPNTEQALRA NFRPCKRCKP TNEKMPDSEW VDLITEYIDK NFTEKLTLES
     LADICHGSPY HMHRTFKKIK GITLVEYIQQ VRVHAAKKYL IQTNKAIGDI AICVGIANAP
     YFITLFKKKT GQTPARFRQM SKMEETYNGN K
//

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