ID ADA_MYCTU Reviewed; 496 AA. AC Q10630; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-JUN-2009, entry version 74. DE RecName: Full=Putative regulatory protein ada; DE AltName: Full=Regulatory protein of adaptative response; DE Includes: DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase; DE EC=2.1.1.63; DE AltName: Full=O-6-methylguanine-DNA alkyltransferase; GN Name=ada; Synonyms=alkA; OrderedLocusNames=Rv1317c, MT1358; GN ORFNames=MTCY130.02c; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh; RX MEDLINE=22206494; PubMed=12218036; RX DOI=10.1128/JB.184.19.5479-5490.2002; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., RA Fraser C.M.; RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL J. Bacteriol. 184:5479-5490(2002). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-496. RC STRAIN=ATCC 25618 / H37Rv; RA Bourn W.R., Harington A., Wiid I., van Helden P.D.; RT "Mycobacterium tuberculosis 3-methyladenine glycosidase and O6- RT methylguanine methyltransferase genes."; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Repair of alkylated guanine in DNA by stoichiometrically CC transferring the alkyl group at the O-6 position to a cysteine CC residue in the enzyme. This is a suicide reaction: the enzyme is CC irreversibly inactivated. Can also repair O-4-methylthymine (By CC similarity). CC -!- FUNCTION: The methylated ADA protein acts as a positive regulator CC of its own synthesis, as well as that of other proteins. The CC transcription-activating function of the ADA protein resides in CC its N-terminus (By similarity). CC -!- CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein CC L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- CC cysteine. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SIMILARITY: In the C-terminal section; belongs to the MGMT family. CC -!- SIMILARITY: Contains 1 HTH araC/xylS-type DNA-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX842576; CAA98104.1; -; Genomic_DNA. DR EMBL; U65786; AAB06751.1; -; Genomic_DNA. DR EMBL; AE000516; AAK45620.1; -; Genomic_DNA. DR PIR; A70769; A70769. DR RefSeq; NP_215833.1; -. DR RefSeq; NP_335806.1; -. DR HSSP; P06134; 1ADN. DR GeneID; 886916; -. DR GeneID; 924701; -. DR GenomeReviews; AE000516_GR; MT1358. DR GenomeReviews; AL123456_GR; Rv1317c. DR KEGG; mtc:MT1358; -. DR KEGG; mtu:Rv1317c; -. DR TIGR; MT1358; -. DR TubercuList; Rv1317c; -. DR HOGENOM; Q10630; -. DR OMA; Q10630; RCRPDSA. DR BRENDA; 2.1.1.63; 809. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methylt...; IEA:EC. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR004026; Ada_DNA_repair_Zn-bd. DR InterPro; IPR010316; AlkA_N. DR InterPro; IPR003583; Helix-hairpin-helix_DNA-bd. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR000005; HTH_AraC-typ. DR InterPro; IPR018062; HTH_AraC-typ_sub_2. DR InterPro; IPR018060; HTH_AraC_domain. DR Gene3D; G3DSA:3.40.10.10; Ada_DNA_repair_Zn-bd; 1. DR Gene3D; G3DSA:3.30.310.20; AlkA_N; 1. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. DR Pfam; PF02805; Ada_Zn_binding; 1. DR Pfam; PF06029; AlkA_N; 1. DR Pfam; PF00730; HhH-GPD; 1. DR Pfam; PF00165; HTH_AraC; 2. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00278; HhH1; 1. DR SMART; SM00342; HTH_ARAC; 1. DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1. DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Metal-binding; Methyltransferase; Transcription; KW Transcription regulation; Transferase; Zinc. FT CHAIN 1 496 Putative regulatory protein ada. FT /FTId=PRO_0000139389. FT DNA_BIND 103 122 H-T-H motif (By similarity). FT COMPBIAS 181 197 Ala-rich. FT ACT_SITE 34 34 Nucleophile; methyl group acceptor from FT phosphotriester (By similarity). FT ACT_SITE 403 403 Nucleophile; methyl group acceptor (By FT similarity). FT METAL 34 34 Zinc (By similarity). FT METAL 38 38 Zinc (By similarity). FT METAL 65 65 Zinc (By similarity). FT METAL 68 68 Zinc (By similarity). FT BINDING 30 30 DNA (By similarity). FT BINDING 41 41 DNA (By similarity). FT BINDING 63 63 DNA (By similarity). SQ SEQUENCE 496 AA; 53743 MW; CA1F52032181268F CRC64; MHDDFERCYR AIQSKDARFD GWFVVAVLTT GVYCRPSCPV RPPFARNVRF LPTAAAAQGE GFRACKRCRP DASPGSPEWN VRSDVVARAM RLIADGTVDR DGVSGLAAQL GYTIRQLERL LQAVVGAGPL ALARAQRMQT ARVLIETTNL PFGDVAFAAG FSSIRQFNDT VRLACDGTPT ALRARAAARF ESATASAGTV SLRLPVRAPF AFEGVFGHLA ATAVPGCEEV RDGAYRRTLR LPWGNGIVSL TPAPDHVRCL LVLDDFRDLM TATARCRRLL DLDADPEAIV EALGADPDLR AVVGKAPGQR IPRTVDEAEF AVRAVLAQQV STKAASTHAG RLVAAYGRPV HDRHGALTHT FPSIEQLAEI DPGHLAVPKA RQRTINALVA SLADKSLVLD AGCDWQRARG QLLALPGVGP WTAEVIAMRG LGDPDAFPAS DLGLRLAAKK LGLPAQRRAL TVHSARWRPW RSYATQHLWT TLEHPVNQWP PQEKIA //