Molecular cloning and sequence analysis of the chitinase gene from Bacillus thuringiensis serovar alesti.
Endogenous chitinase plays a positive role in the pathogenicity of Bacillus thuringiensis to insect pests. The chitinase gene was cloned from B. thuringiensis serovar alesti strain HD-16, and the deduced 676 amino acid sequence showed a high degree of similarity with other Bacillus chitinases. Additionally, the deduced amino acid sequence showed that the protein contained an amino terminus signal peptide and consisted of a catalytic domain, a fibronectin type III domain and a chitin-binding domain. All three domains showed conserved sequences when compared to other bacterial chitinase or cellulase sequences.
Lin
Yi
Y
Department of Bioengineering & Biotechnology, Huaqiao University, Fujian Quanzhou 362011, PR China. lyhxm@hqu.edu.cn
Xiong
Guan
G
D000595:Amino Acid Sequence; D001413:Bacillus thuringiensis / Q000201:enzymology / Q000235:genetics*; D020134:Catalytic Domain / Q000235:genetics; D044602:Cellulases / Q000235:genetics; D002688:Chitinases / Q000235:genetics*; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein
D044602:Cellulases; D002688:Chitinases