%0 Journal Article %A Gleave, Andrew P. %A Hedges, Rebecca J. %A Broadwell, Andrew H. %T Identification of an insecticidal crystal protein from Bacillus thuringiensis DSIR517 with significant sequence differences from previously described toxins %D 1992 %J Microbiology, %V 138 %N 1 %P 55-62 %@ 1465-2080 %R https://doi.org/10.1099/00221287-138-1-55 %I Microbiology Society, %X Summary: The nucleotide (nt) sequence of a DNA segment containing the majority of a gene cloned from Bacillus thuringiensis DSIR517 encoding a 130 kDa insecticidal crystal protein has been determined. Sequence analysis reveals an open reading frame (ORF) of 3453 nt. The ATG initiation codon, which is preceded by a potential ribosome-binding site sequence, was confirmed by N-terminal amino acid sequencing. The ORF extends beyond the 3” terminus of the cloned fragment; however, the high degree of homology between the deduced amino acid sequence of this ORF and other Cry proteins suggests the clone lacks only five C-terminal amino acids. Making this assumption, the ORF of 3468 nt encodes a protein of 1156 amino acids with an estimated molecular mass of 129700 Da. Analysis of the deduced amino acid sequence reveals a number of features characteristic of Cry proteins. Alignment of the Cry 517 protein sequence with other Cry proteins suggests it is most closely related to the crylA-E genes but sufficiently different to form a new cryI gene subclass. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-138-1-55