Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii
Thaller, Maria Cristina and Berlutti, Francesca and Schippa, Serena and Lombardi, Giovanna and Rossolini, Gian Maria,, 140, 1341-1350 (1994),
doi = https://doi.org/10.1099/00221287-140-6-1341,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= Phosphatase activities were investigated in Morganella morganii, 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 p-nitrophenyl phosphate as substrate, Morganella 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, Pi, fluoride and tartrate. The M. morganii PhoC showed 84·6% amino acid sequence identity to the PhoN nonspecific acid phosphatase of Providencia stuartii, 45·3 % to the PhoN nonspecific acid phosphatase of Salmonella typhimurium, and 37·8% to the principal acid phosphatase (PhoC) of Zymomonas mobilis. Comparison of sequence data and of regulation of these enzymes suggested a different phylogeny of members of this gene family within the Enterobacteriaceae.,
language=,
type=