<p>The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) is a major carbohydrate transport system in bacteria. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is as follows: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to Enzyme I (EI) of the PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar- specific permease complex (enzymes EII/EIII).</p><p>HPr is a small cytoplasmic protein, which in some bacteria is found as a domain in a larger protein that includes a EIII(Fru)(IIA) domain and in some cases also a EI domain <db_xref db="INTERPRO" dbkey="IPR000032"/>. HPr is acomponent of the phosphoenolpyruvate-dependent sugar phosphotransferasesystem (PTS) major carbohydrate transport system in bacteria [<cite idref="PUB00003612"/>, <cite idref="PUB00000073"/>].</p><p>There is a conserved histidine in the N terminus of HPr <db_xref db="INTERPRO" dbkey="IPR001020"/>, which serves as an acceptor forthe phosphoryl group of EI. In the central part of HPr there is a conserved serine, which in Gram-positive bacteria only, is phosphorylated by anATP-dependent protein kinase; a process which probably plays a regulatory role in sugartransport.</p><p>The sequence around both phosphorylation sites are well conserved and can be used as signature patterns for HPr proteins or domains. This signature identifies the serine phosporylation site.</p> Phosphotransferase system, HPr serine phosphorylation site