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Protein Domain : IPR036542

Description  The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [ , ] is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of incoming sugar substrates and coupled with translocation across the cell membrane, makes the PTS a link between the uptake and metabolism of sugars.The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred via a signal transduction pathway, to enzyme I (EI) which in turn transfers it to a phosphoryl carrier, the histidine protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease, a membrane-bound complex known as enzyme 2 (EII), which transports the sugar to the cell. EII consists of at least three structurally distinct domains IIA, IIB and IIC [ ]. These can either be fused together in a single polypeptide chain or exist as two or three interactive chains, formerly called enzymes II (EII) and III (EIII).The lactose/cellobiose-specific superfamily are one of four structurally and functionally distinct group IIA PTS system enzymes. This superfamily of proteins normally function as a homotrimer, stabilised by a centrally located metal ion [ ]. Separation into subunits is thought to occur after phosphorylation. It has a spectrin repeat-like fold which consists of three helices arranged in a close bundle with left-handed twist going up-and-down. Name  Phosphotransferase system, lactose/cellobiose-type IIA subunit superfamily
Short Name  PTS_IIA_lac/cel_sf Type  Homologous_superfamily
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Genomics

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