ADA_ECOLI
ID ADA_ECOLI Reviewed; 354 AA.
AC P06134; Q47032;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Bifunctional transcriptional activator/DNA repair enzyme Ada;
DE AltName: Full=Regulatory protein of adaptive response;
DE Includes:
DE RecName: Full=Methylphosphotriester-DNA--protein-cysteine S-methyltransferase;
DE EC=2.1.1.n11 {ECO:0000269|PubMed:2987862};
DE AltName: Full=Methylphosphotriester-DNA methyltransferase;
DE Includes:
DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase;
DE EC=2.1.1.63 {ECO:0000269|PubMed:2987862};
DE AltName: Full=O6-methylguanine-DNA alkyltransferase;
GN Name=ada; OrderedLocusNames=b2213, JW2201;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=2987251; DOI=10.1016/s0021-9258(17)39604-7;
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 [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=3887409; DOI=10.1073/pnas.82.9.2688;
RA Demple B., Sedgwick B., Robins P., Totty N., Waterfield M.D., Lindahl T.;
RT "Active site and complete sequence of the suicidal methyltransferase that
RT counters alkylation mutagenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2688-2692(1985).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX 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., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RC STRAIN=K12;
RX PubMed=2982792; DOI=10.1128/jb.161.3.888-895.1985;
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 agents.";
RL J. Bacteriol. 161:888-895(1985).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-354.
RX PubMed=3536913; DOI=10.1016/s0021-9258(18)66785-7;
RA Kondo H., Nakabeppu Y., Kataoka H., Kuhara S., Kawabata S., Sekiguchi M.;
RT "Structure and expression of the alkB gene of Escherichia coli related to
RT the repair of alkylated DNA.";
RL J. Biol. Chem. 261:15772-15777(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX 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 agents
RT in E. coli.";
RL Cell 45:315-324(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=3529081; DOI=10.1073/pnas.83.17.6297;
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 [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2987862; DOI=10.1093/nar/13.8.2683;
RA McCarthy T.V., Lindahl T.;
RT "Methyl phosphotriesters in alkylated DNA are repaired by the Ada
RT regulatory protein of E. coli.";
RL Nucleic Acids Res. 13:2683-2698(1985).
RN [12]
RP DOMAIN.
RX PubMed=3162236; DOI=10.1016/s0021-9258(18)68944-6;
RA Sedgwick B., Robins P., Totty N., Lindahl T.;
RT "Functional domains and methyl acceptor sites of the Escherichia coli Ada
RT protein.";
RL J. Biol. Chem. 263:4430-4433(1988).
RN [13]
RP ZINC-BINDING.
RX PubMed=1581309; DOI=10.1021/bi00134a002;
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 coli
RT Ada protein.";
RL Biochemistry 31:4541-4547(1992).
RN [14]
RP CHARACTERIZATION.
RX PubMed=8202360; DOI=10.1093/nar/22.9.1613;
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 in
RT DNA.";
RL Nucleic Acids Res. 22:1613-1619(1994).
RN [15]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [16]
RP STRUCTURE BY NMR OF 1-129.
RX PubMed=8500619; DOI=10.1016/0014-5793(93)81351-y;
RA Sakashita H., Sakuma T., Ohkubo T., Kainosho M., Sakumi K., Sekiguchi M.,
RA 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 [17]
RP STRUCTURE BY NMR OF 1-92 IN COMPLEX WITH ZINC IONS.
RX PubMed=8395079; DOI=10.1126/science.8395079;
RA Myers L.C., Terranova M.P., Ferentz A.E., Wagner G., Verdine G.L.;
RT "Repair of DNA methylphosphotriesters through a metalloactivated cysteine
RT nucleophile.";
RL Science 261:1164-1167(1993).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 175-354.
RC STRAIN=B;
RX PubMed=8156986; DOI=10.1002/j.1460-2075.1994.tb06410.x;
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 [19]
RP STRUCTURE BY NMR OF 1-92 IN COMPLEX WITH ZINC IONS, AND INTERACTION WITH
RP DNA.
RX PubMed=11284682; DOI=10.1021/bi002109p;
RA Lin Y., Doetsch V., Wintner T., Peariso K., Myers L.C., Penner-Hahn J.E.,
RA Verdine G.L., Wagner G.;
RT "Structural basis for the functional switch of the E. coli Ada protein.";
RL Biochemistry 40:4261-4271(2001).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 9-139 IN COMPLEX WITH DNA AND ZINC
RP IONS, STRUCTURE BY NMR OF 9-139, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP ACTIVE SITE.
RX PubMed=16209950; DOI=10.1016/j.molcel.2005.08.013;
RA He C., Hus J.-C., Sun L.J., Zhou P., Norman D.P.G., Doetsch V., Wei H.,
RA Gross J.D., Lane W.S., Wagner G., Verdine G.L.;
RT "A methylation-dependent electrostatic switch controls DNA repair and
RT transcriptional activation by E. coli ada.";
RL Mol. Cell 20:117-129(2005).
RN [21]
RP STRUCTURE BY NMR OF 1-146 IN COMPLEX WITH ZINC IONS, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND ACTIVE SITE CYS-38.
RX PubMed=16452614; DOI=10.1110/ps.051786306;
RA Takinowaki H., Matsuda Y., Yoshida T., Kobayashi Y., Ohkubo T.;
RT "The solution structure of the methylated form of the N-terminal 16-kDa
RT domain of Escherichia coli Ada protein.";
RL Protein Sci. 15:487-497(2006).
CC -!- FUNCTION: Involved in the adaptive response to alkylation damage in DNA
CC caused by alkylating agents. Repairs O6-methylguanine (O6-MeG) and O4-
CC methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA
CC by stoichiometrically transferring the methyl group to a cysteine
CC residue in the enzyme (Cys-321). Also specifically repairs the Sp
CC diastereomer of DNA methylphosphotriester lesions by the same
CC mechanism, although the methyl transfer occurs onto a different
CC cysteine residue (Cys-38). Cannot demethylate the other diastereomer,
CC Rp-methylphosphotriester. This is a suicide reaction: the enzyme is
CC irreversibly inactivated. {ECO:0000269|PubMed:2987862}.
CC -!- FUNCTION: The methylation of Ada by methylphosphotriesters in DNA leads
CC to its activation as a transcriptional regulator that activates the
CC transcription of its own gene, ada, and other alkylation resistance
CC genes, alkA, alkB and aidB. {ECO:0000269|PubMed:2987862}.
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:2987862};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein]
CC = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10017,
CC ECO:0000269|PubMed:2987862};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a
CC thymidine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:53428, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, ChEBI:CHEBI:137387;
CC EC=2.1.1.63; Evidence={ECO:0000255|PROSITE-ProRule:PRU10017,
CC ECO:0000269|PubMed:2987862};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- INTERACTION:
CC P06134; P69931: hda; NbExp=3; IntAct=EBI-1119501, EBI-545453;
CC -!- INDUCTION: Up-regulated by methylated Ada itself in response to the
CC exposure to alkylating agents.
CC -!- DOMAIN: Consists of two domains. The 20 kDa N-terminal domain repairs
CC the Sp diastereomer of methylphosphotriesters and, in its methylated
CC form, binds DNA in a sequence-specific manner. The 19 kDa C-terminal
CC domain repairs the mutagenic lesions O6-methylguanine. Each domain
CC retains its activity when separated form the other.
CC {ECO:0000269|PubMed:3162236}.
CC -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and therefore is
CC not strictly catalytic. According to one definition, an enzyme is a
CC biocatalyst that acts repeatedly and over many reaction cycles.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MGMT family.
CC {ECO:0000305}.
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DR EMBL; M10211; AAA23412.1; -; Genomic_DNA.
DR EMBL; M10315; AAA23413.1; -; Genomic_DNA.
DR EMBL; U00008; AAA16408.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75273.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15996.1; -; Genomic_DNA.
DR EMBL; J02607; AAA23415.1; -; Genomic_DNA.
DR EMBL; M13155; AAA23418.1; -; Genomic_DNA.
DR EMBL; M13828; AAA23417.1; -; Genomic_DNA.
DR PIR; C64991; XYECO2.
DR RefSeq; NP_416717.1; NC_000913.3.
DR RefSeq; WP_000710375.1; NZ_LN832404.1.
DR PDB; 1ADN; NMR; -; A=1-92.
DR PDB; 1EYF; NMR; -; A=1-92.
DR PDB; 1SFE; X-ray; 2.10 A; A=175-354.
DR PDB; 1U8B; X-ray; 2.10 A; A=9-139.
DR PDB; 1WPK; NMR; -; A=1-146.
DR PDB; 1ZGW; NMR; -; A=1-139.
DR PDBsum; 1ADN; -.
DR PDBsum; 1EYF; -.
DR PDBsum; 1SFE; -.
DR PDBsum; 1U8B; -.
DR PDBsum; 1WPK; -.
DR PDBsum; 1ZGW; -.
DR AlphaFoldDB; P06134; -.
DR SMR; P06134; -.
DR BioGRID; 4261923; 99.
DR BioGRID; 851051; 4.
DR DIP; DIP-9055N; -.
DR IntAct; P06134; 13.
DR STRING; 511145.b2213; -.
DR jPOST; P06134; -.
DR PaxDb; P06134; -.
DR PRIDE; P06134; -.
DR EnsemblBacteria; AAC75273; AAC75273; b2213.
DR EnsemblBacteria; BAA15996; BAA15996; BAA15996.
DR GeneID; 946710; -.
DR KEGG; ecj:JW2201; -.
DR KEGG; eco:b2213; -.
DR PATRIC; fig|1411691.4.peg.22; -.
DR EchoBASE; EB0028; -.
DR eggNOG; COG0350; Bacteria.
DR eggNOG; COG2169; Bacteria.
DR HOGENOM; CLU_000445_52_0_6; -.
DR InParanoid; P06134; -.
DR OMA; RFAIGQC; -.
DR PhylomeDB; P06134; -.
DR BioCyc; EcoCyc:PD00230; -.
DR BioCyc; MetaCyc:PD00230; -.
DR EvolutionaryTrace; P06134; -.
DR PRO; PR:P06134; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:EcoCyc.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoCyc.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:EcoliWiki.
DR GO; GO:0080111; P:DNA demethylation; IDA:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0018125; P:peptidyl-cysteine methylation; IDA:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd06445; ATase; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.10.10; -; 1.
DR InterPro; IPR035451; Ada-like_dom_sf.
DR InterPro; IPR004026; Ada_DNA_repair_Zn-bd.
DR InterPro; IPR016221; Bifunct_regulatory_prot_Ada.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR InterPro; IPR008332; MethylG_MeTrfase_N.
DR InterPro; IPR036631; MGMT_N_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF02805; Ada_Zn_binding; 1.
DR Pfam; PF01035; DNA_binding_1; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF02870; Methyltransf_1N; 1.
DR PIRSF; PIRSF000409; Ada; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF46767; SSF46767; 1.
DR SUPFAM; SSF53155; SSF53155; 1.
DR SUPFAM; SSF57884; SSF57884; 1.
DR TIGRFAMs; TIGR00589; ogt; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 2.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS00374; MGMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; Metal-binding; Methyltransferase; Multifunctional enzyme;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW Zinc.
FT CHAIN 1..354
FT /note="Bifunctional transcriptional activator/DNA repair
FT enzyme Ada"
FT /id="PRO_0000018747"
FT DOMAIN 85..183
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 102..121
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT REGION 1..171
FT /note="Methylphosphotriester-DNA--protein-cysteine
FT methyltransferase"
FT REGION 181..354
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT ACT_SITE 38
FT /note="Nucleophile; methyl group acceptor from
FT methylphosphotriester"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10017,
FT ECO:0000269|PubMed:16452614"
FT ACT_SITE 321
FT /note="Nucleophile; methyl group acceptor from either O6-
FT methylguanine or O4-methylthymine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10017,
FT ECO:0000269|PubMed:16209950"
FT BINDING 34
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:16209950"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 43
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:16209950"
FT BINDING 45
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:16209950"
FT BINDING 67
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:16209950"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT SITE 128..129
FT /note="Cleavage"
FT SITE 178..179
FT /note="Cleavage"
FT VARIANT 75
FT /note="E -> D (in strain: B)"
FT VARIANT 79..80
FT /note="AQ -> PR (in strain: B)"
FT VARIANT 318
FT /note="I -> V (in strain: B)"
FT VARIANT 330
FT /note="T -> S (in strain: B)"
FT CONFLICT 134
FT /note="A -> R (in Ref. 1; AAA23412)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1ZGW"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:1U8B"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1U8B"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1EYF"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1U8B"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1U8B"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1U8B"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1U8B"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1U8B"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1U8B"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1WPK"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1U8B"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1ADN"
FT HELIX 79..93
FT /evidence="ECO:0007829|PDB:1U8B"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1U8B"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:1U8B"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:1U8B"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:1U8B"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1WPK"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1SFE"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1SFE"
FT STRAND 207..217
FT /evidence="ECO:0007829|PDB:1SFE"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:1SFE"
FT HELIX 240..254
FT /evidence="ECO:0007829|PDB:1SFE"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1SFE"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:1SFE"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:1SFE"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:1SFE"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:1SFE"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:1SFE"
SQ SEQUENCE 354 AA; 39324 MW; 4163E585C768C2F4 CRC64;
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
