The gene encoding the pectin lyase (PNL; EC 4.2.2.10) of Bacillus subtilis has been cloned, sequenced, and characterized. A coding sequence for the PNL composed of 345 amino acids including a 24-amino-acid signal peptide was assigned. No sequence resembling a LexA binding site was found upstream of the structural gene. Furthermore, PNL activity of the gene product expressed in Escherichia coli DH5α was detected intracellularly, which might suggest that expression of the gene was not controlled by RecA. Regulation of the gene expression seemed to be quite different from that of other bacterial PNL genes previously reported.
