Molecular cloning, expression and nucleotide sequence of the endo‐β‐1,3‐1,4‐d‐glucanase gene from Bacillus licheniformis Predictive structural analyses of the encoded polypeptide

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Abstract
A Bacillus licheniformis gene coding for an endo‐β‐1,3‐1,4‐d‐glucanase have been cloned in Escherichia coli and sequenced. The open reading frame contains a sequence of 731 bp, encoding a polypeptide of 243 amino acid residues, with a molecular mass of 27404 Da (24418 Da without the putative signal peptide), which corresponds to the enzyme we had previously isolated and characterized. The signal peptide is functional in E. coli. More than 60% of the endo‐β‐1,3‐1,4‐d‐glucanase activity is extracellular or periplasmic. The polypeptide is highly similar to other reported Bacillus β‐glucanases. Several structural predictive analyses (secondary structure, hydropathic plots, similarity with other related enzymes, etc.) have been performed. From these analyses we assign a tentative three‐functional‐domain structure for the enzyme (signal peptide, substrate binding and catalytic domains) and a putative lysozyme‐like active site.