title: Cloning and characterization of the NapA acid phosphatase/phosphotransferase of Morganella morganii: identification of a new family of bacterial acid-phosphatase-encoding genes.
abstract: The gene encoding a minor phosphate-irrepressible acid phosphatase (named NapA) of Morganella morganii was cloned and sequenced, and its product characterized. NapA is a secreted acid phosphatase composed of four 27 kDa polypeptide subunits. The enzyme is active on several organic phosphate monoesters but not on diesters, and is also endowed with transphosphorylating activity from organic phosphoric acid esters to nucleosides and other compounds with free hydroxyl groups. Its activity is inhibited by EDTA, inorganic phosphate, nucleosides and Ca2+, but not by fluoride or tartrate, and is enhanced by Mg2+, Co2+ and Zn2+. At the sequence level, the NapA enzyme did not show similarities to any other sequenced bacterial phosphatases. However, a search for homologous genes in sequence databases allowed identification of two open reading frames located within sequenced regions of the Escherichia coli and Proteus mirabilis genomes respectively, encoding proteins of unknown function which are highly homologous to the Morganella enzyme. Moreover, the properties of the NapA enzyme are very similar to those reported for the periplasmic nonspecific acid phosphatase II of Salmonella typhimurium (for which no sequence data are available). These data point to the existence of a new family of bacterial acid phosphatases, which we propose designating class B bacterial acid phosphatases.
authors.affiliation: Istituto di Microbiologia, Università La Sapienza, Rome, Italy.
authors.forename: M C
authors.initials: MC
authors.lastname: Thaller
authors.forename: G
authors.initials: G
authors.lastname: Lombardi
authors.forename: F
authors.initials: F
authors.lastname: Berlutti
authors.forename: S
authors.initials: S
authors.lastname: Schippa
authors.forename: G M
authors.initials: GM
authors.lastname: Rossolini
mesh_terms: D000135:Acid Phosphatase / Q000096:biosynthesis* / Q000235:genetics* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D001483:Base Sequence; D002413:Cations, Divalent / Q000494:pharmacology; D003001:Cloning, Molecular; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004755:Enterobacteriaceae / Q000201:enzymology* / Q000235:genetics*; D004926:Escherichia coli; D005798:Genes, Bacterial; D007700:Kinetics; D008969:Molecular Sequence Data; D005810:Multigene Family; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism; D015183:Restriction Mapping; D012486:Salmonella typhimurium / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D002413:Cations, Divalent; D011994:Recombinant Proteins; D004492:Edetic Acid; D000135:Acid Phosphatase; C092729:NapA phosphatase