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   25-MAY-2022, entry version 55.
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; Firmicutes; 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}.
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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; -; 1.
DR   InterPro; IPR035918; CytB_endotoxin-like_sf.
DR   InterPro; IPR001615; Endotoxin_CytB.
DR   Pfam; PF01338; Bac_thur_toxin; 1.
DR   SUPFAM; SSF55676; SSF55676; 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