ID CT1AA_BACTI Reviewed; 249 AA. AC P0A382; P05069; P05628; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 08-NOV-2023, entry version 60. DE RecName: Full=Type-1Aa cytolytic delta-endotoxin; DE AltName: Full=27 kDa cytolytic toxin; GN Name=cyt1Aa; Synonyms=cytA; OS Bacillus thuringiensis subsp. israelensis. OG Plasmid 72 Kb. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1430; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3025452; DOI=10.1016/0022-2836(86)90417-1; RA Ward E.S., Ellar D.J.; RT "Bacillus thuringiensis var. israelensis delta-endotoxin. Nucleotide RT sequence and characterization of the transcripts in Bacillus thuringiensis RT and Escherichia coli."; RL J. Mol. Biol. 191:1-11(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3025453; DOI=10.1016/0022-2836(86)90418-3; RA Ward E.S., Ridley A.R., Ellar D.J., Todd J.A.; RT "Bacillus thuringiensis var. israelensis delta-endotoxin. Cloning and RT expression of the toxin in sporogenic and asporogenic strains of Bacillus RT subtilis."; RL J. Mol. Biol. 191:13-22(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS. RX PubMed=2845100; DOI=10.1016/0022-2836(88)90283-5; RA Ward E.S., Ellar D.J., Chilcott C.N.; RT "Single amino acid changes in the Bacillus thuringiensis var. israelensis RT delta-endotoxin affect the toxicity and expression of the protein."; RL J. Mol. Biol. 202:527-535(1988). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=4070003; DOI=10.1093/nar/13.22.8207; RA Waalwijk C., Dullemans A.M., van Workum M.E.S., Visser B.; RT "Molecular cloning and the nucleotide sequence of the Mr 28 000 crystal RT protein gene of Bacillus thuringiensis subsp. israelensis."; RL Nucleic Acids Res. 13:8207-8217(1985). RN [5] RP SEQUENCE REVISION TO 34-35. RA Waalwijk C.; RL Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Kills the larvae of dipteran insects by making pores in the CC epithelial cell membrane of the insect midgut. Acts on mosquitos and CC black flies. CC -!- DEVELOPMENTAL STAGE: The crystal protein is produced during sporulation CC and is accumulated both as an inclusion and as part of the spore coat. CC -!- PTM: Active after proteolytic processing. CC -!- SIMILARITY: Belongs to the cyt1/cyt2 endotoxin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04338; CAA27868.1; -; Genomic_DNA. DR EMBL; X03182; CAA26943.1; -; Genomic_DNA. DR PIR; A24044; A24044. DR RefSeq; WP_000429377.1; NZ_VEIF01000045.1. DR PDB; 3RON; X-ray; 2.19 A; A/B=1-249. DR PDB; 6T14; X-ray; 1.86 A; BBB=1-249. DR PDB; 6T19; X-ray; 1.85 A; BBB=1-249. DR PDB; 6T1A; X-ray; 1.85 A; BBB=1-249. DR PDB; 6T1C; X-ray; 2.00 A; BBB=1-249. DR PDBsum; 3RON; -. DR PDBsum; 6T14; -. DR PDBsum; 6T19; -. DR PDBsum; 6T1A; -. DR PDBsum; 6T1C; -. DR AlphaFoldDB; P0A382; -. DR SMR; P0A382; -. DR TCDB; 1.C.71.1.1; the cytolytic delta endotoxin (cyt1/2) family. DR EvolutionaryTrace; P0A382; -. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. DR Gene3D; 3.40.198.10; Delta-endotoxin CytB-like; 1. DR InterPro; IPR035918; CytB_endotoxin-like_sf. DR InterPro; IPR001615; Endotoxin_CytB. DR Pfam; PF01338; Bac_thur_toxin; 1. DR SUPFAM; SSF55676; CytB endotoxin-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Plasmid; Sporulation; Toxin; Virulence. FT CHAIN 1..249 FT /note="Type-1Aa cytolytic delta-endotoxin" FT /id="PRO_0000174104" FT STRAND 40..47 FT /evidence="ECO:0007829|PDB:3RON" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:3RON" FT HELIX 52..62 FT /evidence="ECO:0007829|PDB:3RON" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:3RON" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:3RON" FT TURN 71..73 FT /evidence="ECO:0007829|PDB:3RON" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:3RON" FT HELIX 81..90 FT /evidence="ECO:0007829|PDB:3RON" FT STRAND 96..111 FT /evidence="ECO:0007829|PDB:3RON" FT HELIX 112..127 FT /evidence="ECO:0007829|PDB:3RON" FT HELIX 129..134 FT /evidence="ECO:0007829|PDB:3RON" FT HELIX 136..147 FT /evidence="ECO:0007829|PDB:3RON" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:3RON" FT STRAND 159..165 FT /evidence="ECO:0007829|PDB:3RON" FT STRAND 168..181 FT /evidence="ECO:0007829|PDB:3RON" FT TURN 182..186 FT /evidence="ECO:0007829|PDB:3RON" FT STRAND 187..201 FT /evidence="ECO:0007829|PDB:3RON" FT HELIX 203..206 FT /evidence="ECO:0007829|PDB:3RON" FT STRAND 214..229 FT /evidence="ECO:0007829|PDB:3RON" SQ SEQUENCE 249 AA; 27341 MW; E661946298D3989A CRC64; MENLNHCPLE DIKVNPWKTP QSTARVITLR VEDPNEINNL LSINEIDNPN YILQAIMLAN AFQNALVPTS TDFGDALRFS MPKGLEIANT ITPMGAVVSY VDQNVTQTNN QVSVMINKVL EVLKTVLGVA LSGSVIDQLT AAVTNTFTNL NTQKNEAWIF WGKETANQTN YTYNVLFAIQ NAQTGGVMYC VPVGFEIKVS AVKEQVLFFT IQDSASYNVN IQSLKFAQPL VSSSQYPIAD LTSAINGTL //