A gene (designated ldcC) mapped at 4.6 min on the Escherichia coli chromosome codes for a protein of 713 amino acids (aa) that shows strong similarities in both size and amino-acid sequence (69% identical residues and 85% conserved residues) to lysine decarboxylase (LDC) from E. coli (CadA, acid-inducible LDC, 715 aa) or from Hafnia alvei (739 aa). A pUC18 derivative carrying the ldcC gene conferred high LDC activities on an E. coli strain devoid of the functional cadA gene, even when the bacteria were grown under non-inducing conditions at physiological pH. Thus, the gene encodes another lysine decarboxylase, probably a constitutively expressed enzyme, the presence of which was suggested from the previous observations that low LDC activities were detectable in cadA^- mutant and non-induced wild-type cells.