Reviewed,
UniProtKB/Swiss-Prot P06134 (ADA_ECOLI)
Last modified
June 16, 2009.
Version 110.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Regulatory protein ada Alternative name(s): Regulatory protein of adaptative response Cleaved into the following chain: 1- Recommended name: Methylated-DNA--protein-cysteine methyltransferase EC=2.1.1.63 Alternative name(s): O-6-methylguanine-DNA alkyltransferase | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 354 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Repair of alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. Can also repair O-4-methylthymine. The methylated ADA protein acts as a positive regulator of its own synthesis, as well as that of other proteins. The transcription-activating function of the ADA protein resides in its N-terminus. It activates the transcription of alkA, alkB and aidB. |
| Catalytic activity | DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine. |
| Cofactor | Binds 1 zinc ion per subunit. |
| Sequence similarities | In the C-terminal section; belongs to the MGMT family. Contains 1 HTH araC/xylS-type DNA-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA repair Transcription Transcription regulation |
| Ligand | DNA-binding Metal-binding Zinc |
| Molecular function | Activator Methyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | DNA repair Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | intracellular Inferred from electronic annotation. Source: InterPro |
| Molecular function | methylated-DNA-[protein]-cysteine S-methyltransferase activity Inferred from electronic annotation. Source: EC sequence-specific DNA bindingInferred from electronic annotation. Source: InterPro transcription factor activityInferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 354 | 354 | Regulatory protein ada | PRO_0000018747 | |||||||||||||||||||||||||||||||||||||||||||
| Chain | 179 – 354 | 176 | Methylated-DNA--protein-cysteine methyltransferase | PRO_0000018748 | |||||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||||||
| DNA binding | 102 – 121 | 20 | H-T-H motif | ||||||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 38 | 1 | Nucleophile; methyl group acceptor from phosphotriester Ref.17 Ref.18 | ||||||||||||||||||||||||||||||||||||||||||||
| Active site | 321 | 1 | Nucleophile; methyl group acceptor Ref.17 Ref.18 | ||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 38 | 1 | Zinc | ||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 42 | 1 | Zinc | ||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 69 | 1 | Zinc | ||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 72 | 1 | Zinc | ||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 34 | 1 | DNA | ||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 43 | 1 | DNA | ||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 45 | 1 | DNA | ||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 67 | 1 | DNA | ||||||||||||||||||||||||||||||||||||||||||||
| Site | 128 – 129 | 2 | Cleavage | ||||||||||||||||||||||||||||||||||||||||||||
| Site | 178 – 179 | 2 | Cleavage | ||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 75 | 1 | E → D in strain: B. | ||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 79 – 80 | 2 | AQ → PR in strain: B. | ||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 318 | 1 | I → V in strain: B. | ||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 330 | 1 | T → S in strain: B. | ||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 134 | 1 | A → R in AAA23412. Ref.1 | ||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 9 – 17 | 9 | |||||||||||||||||||||||||||||||||||||||||||||
| Turn | 24 – 26 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 28 – 31 | 4 | |||||||||||||||||||||||||||||||||||||||||||||
| Turn | 32 – 34 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 36 – 38 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 49 – 51 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 52 – 57 | 6 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 58 – 63 | 6 | |||||||||||||||||||||||||||||||||||||||||||||
| Turn | 70 – 72 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 79 – 81 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 190 – 196 | 7 | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 199 – 205 | 7 | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 207 – 217 | 11 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 219 – 229 | 11 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 240 – 254 | 15 | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 255 – 257 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 270 – 279 | 10 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 290 – 296 | 7 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 303 – 311 | 9 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 321 – 323 | 3 | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 338 – 348 | 11 | |||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Purification and structure of the intact Ada regulatory protein of Escherichia coli K12, O6-methylguanine-DNA methyltransferase." Nakabeppu Y., Kondo H., Kawabata S., Iwanaga S., Sekiguchi M. J. Biol. Chem. 260:7281-7288(1985) [PubMed: 2987251] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12. |
| [2] | "Active site and complete sequence of the suicidal methyltransferase that counters alkylation mutagenesis." Demple B., Sedgwick B., Robins P., Totty N., Waterfield M.D., Lindahl T. Proc. Natl. Acad. Sci. U.S.A. 82:2688-2692(1985) [PubMed: 3887409] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B. |
| [3] | "Automated multiplex sequencing of the E.coli genome." Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M. Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / BHB2600. |
| [4] | "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T.DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [6] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [7] | "Induction and autoregulation of ada, a positively acting element regulating the response of Escherichia coli K-12 to methylating agents." Lemotte P.K., Walker G.C. J. Bacteriol. 161:888-895(1985) [PubMed: 2982792] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49. Strain: K12. |
| [8] | "Structure and expression of the alkB gene of Escherichia coli related to the repair of alkylated DNA." Kondo H., Nakabeppu Y., Kataoka H., Kuhara S., Kawabata S., Sekiguchi M. J. Biol. Chem. 261:15772-15777(1986) [PubMed: 3536913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-354. |
| [9] | "The intracellular signal for induction of resistance to alkylating agents in E. coli." Teo I., Sedgwick B., Kilpatrick M.W., McCarthy T.V., Lindahl T. Cell 45:315-324(1986) [PubMed: 3009022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. |
| [10] | "Regulatory mechanisms for induction of synthesis of repair enzymes in response to alkylating agents: ada protein acts as a transcriptional regulator." Nakabeppu Y., Sekiguchi M. Proc. Natl. Acad. Sci. U.S.A. 83:6297-6301(1986) [PubMed: 3529081] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27. |
| [11] | "Zinc binding by the methylation signaling domain of the Escherichia coli Ada protein." Myers L.C., Terranova M.P., Nash H.M., Markus M.A., Verdine G.L. Biochemistry 31:4541-4547(1992) [PubMed: 1581309] [Abstract] Cited for: ZINC-BINDING. |
| [12] | "Specificities of human, rat and E. coli O6-methylguanine-DNA methyltransferases towards the repair of O6-methyl and O6-ethylguanine in DNA." Liem L.-K., Lim A., Li B.F.L. Nucleic Acids Res. 22:1613-1619(1994) [PubMed: 8202360] [Abstract] Cited for: CHARACTERIZATION. |
| [13] | "Folding topology and DNA binding of the N-terminal fragment of Ada protein." Sakashita H., Sakuma T., Ohkubo T., Kainosho M., Sakumi K., Sekiguchi M., Morikawa K. FEBS Lett. 323:252-256(1993) [PubMed: 8500619] [Abstract] Cited for: STRUCTURE BY NMR OF 1-129. |
| [14] | "Repair of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile." Myers L.C., Terranova M.P., Ferentz A.E., Wagner G., Verdine G.L. Science 261:1164-1167(1993) [PubMed: 8395079] [Abstract] Cited for: STRUCTURE BY NMR OF 1-92 IN COMPLEX WITH ZINC IONS. |
| [15] | "Crystal structure of a suicidal DNA repair protein: the Ada O6-methylguanine-DNA methyltransferase from E. coli." Moore M.H., Gulbis J.M., Dodson E.J., Demple B., Moody P.C.E. EMBO J. 13:1495-1501(1994) [PubMed: 8156986] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 175-354. Strain: B. |
| [16] | "Structural basis for the functional switch of the E. coli Ada protein." Lin Y., Doetsch V., Wintner T., Peariso K., Myers L.C., Penner-Hahn J.E., Verdine G.L., Wagner G. Biochemistry 40:4261-4271(2001) [PubMed: 11284682] [Abstract] Cited for: STRUCTURE BY NMR OF 1-92 IN COMPLEX WITH ZINC IONS, INTERACTION WITH DNA. |
| [17] | "A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli ada." He C., Hus J.-C., Sun L.J., Zhou P., Norman D.P.G., Doetsch V., Wei H., Gross J.D., Lane W.S., Wagner G., Verdine G.L. Mol. Cell 20:117-129(2005) [PubMed: 16209950] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 9-139 IN COMPLEX WITH DNA AND ZINC IONS, STRUCTURE BY NMR OF 9-139, MASS SPECTROMETRY, ACTIVE SITE. |
| [18] | "The solution structure of the methylated form of the N-terminal 16-kDa domain of Escherichia coli Ada protein." Takinowaki H., Matsuda Y., Yoshida T., Kobayashi Y., Ohkubo T. Protein Sci. 15:487-497(2006) [PubMed: 16452614] [Abstract] Cited for: STRUCTURE BY NMR OF 1-146 IN COMPLEX WITH ZINC IONS, MASS SPECTROMETRY, ACTIVE SITE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M10211 Genomic DNA. Translation: AAA23412.1. M10315 Genomic DNA. Translation: AAA23413.1. U00008 Genomic DNA. Translation: AAA16408.1. U00096 Genomic DNA. Translation: AAC75273.1. AP009048 Genomic DNA. Translation: BAA15996.1. J02607 Genomic DNA. Translation: AAA23415.1. M13155 Genomic DNA. Translation: AAA23418.1. M13828 Genomic DNA. Translation: AAA23417.1. | |||||||||||||||||||||||||||||||||||||||||||
| PIR | XYECO2. C64991. | ||||||||||||||||||||||||||||||||||||||||||
| RefSeq | AP_002809.1. NP_416717.1. | ||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||||||||||||||
| DIP | DIP:9055N. | ||||||||||||||||||||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||||||||||||||||||||
| AraC-XylS | Search... | ||||||||||||||||||||||||||||||||||||||||||
2-D gel databases | |||||||||||||||||||||||||||||||||||||||||||
| ECO2DBASE | I039.5. 6TH EDITION. | ||||||||||||||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||||||||||||||
| GeneID | 946710. | ||||||||||||||||||||||||||||||||||||||||||
| GenomeReviews | Gene locus JW2201 in contig AP009048_GR. Gene locus b2213 in contig U00096_GR. | ||||||||||||||||||||||||||||||||||||||||||
| KEGG | ecj:JW2201. eco:b2213. | ||||||||||||||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||||||||||||||
| EchoBASE | EB0028. | ||||||||||||||||||||||||||||||||||||||||||
| EcoGene | EG10029. ada. | ||||||||||||||||||||||||||||||||||||||||||
| CMR | Search... | ||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||
| HOGENOM | P06134. | ||||||||||||||||||||||||||||||||||||||||||
| OMA | P06134. SNSRFYE. | ||||||||||||||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||||||||||||||
| BioCyc | EcoCyc:PD00230. | ||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR004026. Ada_DNA_repair_Zn-bd. IPR016221. Bifunct_regulatory_prot_Ada. IPR000005. HTH_AraC-typ. IPR018062. HTH_AraC-typ_sub_2. IPR018060. HTH_AraC_domain. IPR001497. MethylDNA_cys_MeTrfase_AS. IPR014048. MethylDNA_cys_MeTrfase_DNA_bd. IPR008332. MethylG_MeTrfase. IPR011991. Wing_hlx_DNA_bd. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| Gene3D | G3DSA:3.40.10.10. Ada_DNA_repair_Zn-bd. 1 hit. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| PANTHER | PTHR10815. MethylDNA_cys_mtrans_DNA_bd. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| Pfam | PF02805. Ada_Zn_binding. 1 hit. PF01035. DNA_binding_1. 1 hit. PF00165. HTH_AraC. 2 hits. PF02870. Methyltransf_1N. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| PIRSF | PIRSF000409. Ada. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| SMART | SM00342. HTH_ARAC. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| TIGRFAMs | TIGR00589. ogt. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| PROSITE | PS00041. HTH_ARAC_FAMILY_1. 2 hits. PS01124. HTH_ARAC_FAMILY_2. 1 hit. PS00374. MGMT. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | ADA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P06134 Secondary accession number(s): Q47032 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


