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Description:
Regulatory protein ada (Regulatory protein of adaptative response)[Contains: Methylated-DNA--protein-cysteine methyltransferase(EC 2.1.1.63) (O-6-methylguanine-DNA alkyltransferase)].
Molecular weight: 39324
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
07-MAR-2006, entry version 78.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein ADA_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M10211 | AAA23412.1 | - |
| EMBL | M10315 | AAA23413.1 | - |
| EMBL | J02607 | AAA23415.1 | - |
| EMBL | M13155 | AAA23418.1 | - |
| EMBL | U00008 | AAA16408.1 | - |
| EMBL | U00096 | AAC75273.1 | - |
| EMBL | D90850 | BAA15996.1 | - |
| EMBL | M13828 | AAA23417.1 | - |
| PIR | C64991 | XYECO2. | |
| PDB | 1ADN | NMR | @=1-92. |
| PDB | 1EYF | NMR | A=1-92. |
| PDB | 1SFE | X-ray | @=175-354. |
| PDB | 1U8B | X-ray | A=9-139. |
| PDB | 1WPK | NMR | A=1-146. |
| PDB | 1ZGW | NMR | A=1-139. |
| ECO2DBASE | I039.5 | 6TH EDITION. | |
| GenomeReviews | U00096_GR | b2213.1 | |
| EchoBASE | EB0028 | -.1 | |
| EcoGene | EG10029 | ada. | |
| BioCyc | EcoCyc:PD00230 | -.1 | |
| LinkHub | P06134 | -.1 | |
| InterPro | IPR004026 | Ada_Zn_bd. | |
| InterPro | IPR000005 | HTHAraC. | |
| InterPro | IPR008332 | MethylG_mtfrase. | |
| InterPro | IPR001497 | Methyltransf_1. | |
| InterPro | IPR011991 | Wing_hlx_DNA_bd. | |
| Pfam | PF02805 | Ada_Zn_binding | 1. |
| Pfam | PF01035 | DNA_binding_1 | 1. |
| Pfam | PF00165 | HTH_AraC | 2. |
| Pfam | PF02870 | Methyltransf_1N | 1. |
| PRINTS | PR00032 | HTHARAC. | |
| SMART | SM00342 | HTH_ARAC | 1. |
| TIGRFAMs | TIGR00589 | ogt | 1. |
| PROSITE | PS00041 | HTH_ARAC_FAMILY_1 | 2. |
| PROSITE | PS01124 | HTH_ARAC_FAMILY_2 | 1. |
| PROSITE | PS00374 | MGMT | 1. |
Keywords:
3D-structure; Activator; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA-binding; Metal-binding; Methyltransferase; Transcription; Transcription regulation; Transferase; Zinc.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX MEDLINE=85207761; PubMed=2987251;
RA Nakabeppu Y., Kondo H., Kawabata S., Iwanaga S., Sekiguchi M.;
RT "Purification and structure of the intact Ada regulatory protein of
RT Escherichia coli K12, O6-methylguanine-DNA methyltransferase.";
RL J. Biol. Chem. 260:7281-7288(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=97251358; PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
RA Yamamoto Y., Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX MEDLINE=85190562; PubMed=3887409;
RA Demple B., Sedgwick B., Robins P., Totty N., Waterfield M.D.,
RA Lindahl T.;
RT "Active site and complete sequence of the suicidal methyltransferase
RT that counters alkylation mutagenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2688-2692(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RC STRAIN=K12;
RX MEDLINE=85130822; PubMed=2982792;
RA Lemotte P.K., Walker G.C.;
RT "Induction and autoregulation of ada, a positively acting element
RT regulating the response of Escherichia coli K-12 to methylating
RT agents.";
RL J. Bacteriol. 161:888-895(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-354.
RX MEDLINE=87057220; PubMed=3536913;
RA Kondo H., Nakabeppu Y., Kataoka H., Kuhara S., Kawabata S.,
RA Sekiguchi M.;
RT "Structure and expression of the alkB gene of Escherichia coli related
RT to the repair of alkylated DNA.";
RL J. Biol. Chem. 261:15772-15777(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX MEDLINE=86189944; PubMed=3009022; DOI=10.1016/0092-8674(86)90396-X;
RA Teo I., Sedgwick B., Kilpatrick M.W., McCarthy T.V., Lindahl T.;
RT "The intracellular signal for induction of resistance to alkylating
RT agents in E. coli.";
RL Cell 45:315-324(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX MEDLINE=86313568; PubMed=3529081;
RA Nakabeppu Y., Sekiguchi M.;
RT "Regulatory mechanisms for induction of synthesis of repair enzymes in
RT response to alkylating agents: ada protein acts as a transcriptional
RT regulator.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6297-6301(1986).
RN [10]
RP ZINC-BINDING.
RX MEDLINE=92256385; PubMed=1581309;
RA Myers L.C., Terranova M.P., Nash H.M., Markus M.A., Verdine G.L.;
RT "Zinc binding by the methylation signaling domain of the Escherichia
RT coli Ada protein.";
RL Biochemistry 31:4541-4547(1992).
RN [11]
RP STRUCTURE BY NMR OF 1-129.
RX MEDLINE=93272965; PubMed=8500619; DOI=10.1016/0014-5793(93)81351-Y;
RA Sakashita H., Sakuma T., Ohkubo T., Kainosho M., Sakumi K.,
RA Sekiguchi M., Morikawa K.;
RT "Folding topology and DNA binding of the N-terminal fragment of Ada
RT protein.";
RL FEBS Lett. 323:252-256(1993).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 175-354.
RC STRAIN=B;
RX MEDLINE=94208516; PubMed=8156986;
RA Moore M.H., Gulbis J.M., Dodson E.J., Demple B., Moody P.C.E.;
RT "Crystal structure of a suicidal DNA repair protein: the Ada O6-
RT methylguanine-DNA methyltransferase from E. coli.";
RL EMBO J. 13:1495-1501(1994).
RN [13]
RP CHARACTERIZATION.
RX MEDLINE=94261426; PubMed=8202360;
RA Liem L.-K., Lim A., Li B.F.L.;
RT "Specificities of human, rat and E. coli O6-methylguanine-DNA
RT methyltransferases towards the repair of O6-methyl and O6-ethylguanine
RT in DNA.";
RL Nucleic Acids Res. 22:1613-1619(1994).
Feature:
CHAIN 1 354 Regulatory protein ada.
/FTId=PRO_0000018747.
CHAIN 179 354 Methylated-DNA--protein-cysteine
methyltransferase.
/FTId=PRO_0000018748.
DNA_BIND 102 121 H-T-H motif (By similarity).
ACT_SITE 69 69 Acceptor for methyl from phosphotriester.
ACT_SITE 321 321 Alkyl group acceptor.
METAL 38 38 Zinc (Probable).
METAL 42 42 Zinc (Probable).
METAL 69 69 Zinc (Probable).
METAL 72 72 Zinc (Probable).
SITE 128 129 Cleavage.
SITE 178 179 Cleavage.
VARIANT 75 75 E -> D (in strain: B).
VARIANT 79 80 AQ -> PR (in strain: B).
VARIANT 318 318 I -> V (in strain: B).
VARIANT 330 330 T -> S (in strain: B).
CONFLICT 134 134 A -> R (in Ref. 1).
STRAND 4 5
HELIX 9 18
STRAND 19 20
STRAND 22 23
TURN 25 26
STRAND 28 31
TURN 32 35
STRAND 36 38
STRAND 40 40
STRAND 44 45
STRAND 49 57
HELIX 58 64
TURN 65 65
STRAND 68 71
STRAND 76 78
TURN 79 81
STRAND 85 87
STRAND 90 90
STRAND 190 196
TURN 197 198
STRAND 199 205
STRAND 207 217
HELIX 219 229
STRAND 230 230
TURN 231 232
STRAND 234 235
TURN 237 238
HELIX 240 254
STRAND 255 257
STRAND 262 262
STRAND 264 264
STRAND 268 268
HELIX 270 279
TURN 280 281
STRAND 282 282
TURN 284 285
STRAND 288 289
HELIX 290 296
TURN 297 298
TURN 300 301
HELIX 303 311
TURN 312 312
STRAND 315 316
TURN 317 318
STRAND 319 319
HELIX 321 323
STRAND 324 325
TURN 327 328
STRAND 329 329
TURN 332 333
TURN 335 336
HELIX 338 348
STRAND 349 349
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.
-!- FUNCTION: 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.
-!- SIMILARITY: In the C-terminal section; belongs to the MGMT family.
-!- SIMILARITY: Contains 1 HTH araC/xylS-type DNA-binding domain.
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Sequence length: 354
MKKATCLTDD QRWQSVLARD PNADGEFVFA VRTTGIFCRP SCRARHALRE NVSFYANASE
ALAAGFRPCK RCQPEKANAQ QHRLDKITHA CRLLEQETPV TLEALADQVA MSPFHLHRLF
KATTGMTPKA WQQAWRARRL RESLAKGESV TTSILNAGFP DSSSYYRKAD ETLGMTAKQF
RHGGENLAVR YALADCELGR CLVAESERGI CAILLGDDDA TLISELQQMF PAADNAPADL
MFQQHVREVI ASLNQRDTPL TLPLDIRGTA FQQQVWQALR TIPCGETVSY QQLANAIGKP
KAVRAVASAC AANKLAIIIP CHRVVRGDGT LSGYRWGVSR KAQLLRREAE NEER