Phosphatase activities were investigated in , which is one of the few enterobacterial species producing high-level phosphateirrepressible acid phosphatase activity (HPAP phenotype), and the gene encoding the major phosphate-irrepressible acid phosphatase was cloned, sequenced, and its product characterized. Using -nitrophenyl phosphate as substrate, produced a major phosphate-irrepressible acid phosphatase (named PhoC) which is associated with the HPAP phenotype, a minor phosphate-irrepressible acid phosphatase, and a phosphate-repressible alkaline phosphatase. The presence of the PhoC activity prevented induction of alkaline phosphatase when a PhoC-hydrolysable organic phosphate ester, such as glycerol 2-phosphate, was the sole phosphate source. PhoC is a secreted nonspecific acid phosphatase apparently composed of four 25 kDa polypeptide subunits. The enzyme is resistant to EDTA, P, fluoride and tartrate. The PhoC showed 84.6% amino acid sequence identity to the PhoN nonspecific acid phosphatase of , 45.3 % to the PhoN nonspecific acid phosphatase of , and 37.8% to the principal acid phosphatase (PhoC) of . Comparison of sequence data and of regulation of these enzymes suggested a different phylogeny of members of this gene family within the .


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