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 03-AUG-2022, entry version 154.
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=(2'-deoxyribonucleoside 5'-methylphosphotriester)-DNA + L-
CC cysteinyl-[protein] = 2'-deoxyribonucleotide-DNA + H(+) + S-methyl-L-
CC 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}.
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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 AlphaFoldDB; P19219; -.
DR SMR; P19219; -.
DR STRING; 224308.BSU01810; -.
DR PaxDb; P19219; -.
DR PRIDE; P19219; -.
DR EnsemblBacteria; CAB11957; CAB11957; BSU_01810.
DR GeneID; 938648; -.
DR KEGG; bsu:BSU01810; -.
DR PATRIC; fig|224308.179.peg.187; -.
DR eggNOG; COG2169; Bacteria.
DR InParanoid; P19219; -.
DR OMA; PYHLQRT; -.
DR PhylomeDB; P19219; -.
DR BioCyc; BSUB:BSU01810-MON; -.
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;
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 BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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
