Sy. Wang et al., Molecular cloning and structural analysis of the gene encoding Bacillus cereus exochitinase Chi36, J BIOSCI BI, 92(1), 2001, pp. 59-66
The chi36 gene encoding exochitinase Chi36 was cloned from a Bacillus cereu
s 6E1 subgenomic library. The chi36 open reading frame is 1080 bp long enco
ding a Chi36 precursor protein of 360 amino acids, consisting of a 27 amino
acid N-terminal signal peptide and a 333 amino acid sequence found in the
mature Chi36 protein of 36.346 kDa. Chi36 shows significant amino acid sequ
ence similarity to many bacterial chitinases, but has highest similarity to
B. circulans WL-12 chitinase D. Chi36 belongs to subfamily B of bacterial
chitinases in family 18 of glycosyl hydrolases. Chi36 shows a simple and co
mpact structural organization composed of an N-terminal signal peptide and
a C-terminal (beta/(alpha)(8)-barrel catalytic domain (CaD). The Chi36 sign
al peptide is recognized by Escherichia coli, allowing Chi36 secretion. Chi
36 is the first one-domain (CaD) bacterial chitinase cloned from B. cereus.