The gene encoding endo-beta-1,4-glucanase in Bacillus subtilis CK-2 was cloned into Escherichia coli DH5 alpha, and the nucleotide sequence determined. The 1500 bp gene encodes a protein of 499 amino-acid residues with a calculated molecular mass of 55,261, and is equipped with a typical B. subtilis signal peptide. Nucleotide sequence comparison revealed only 2 basepairs deviation between this gene and the endo-beta-1,4-glucanase gene of B. subtilis PAP115, and 93% to 95% homology was found between the amino acid sequences of these enzymes and other B. subtilis endo-beta-1,4-glucanases. Regions of similarity were also observed between the carboxy-terminal part of these enzymes and the part of the B. lautus PL236 celA enzyme constituting the cellulose-binding domain.