| Primary Identifier | IPR037414 | Type | Domain |
| Short Name | LysR_PBP2 |
| description | LysR is the transcriptional activator of lysA, a diaminopimelate decarboxylase that catalyses the decarboxylation of diaminopimelate to produce lysine. The C-terminal substrate-binding domain of LysR shows significant homology to the type 2 periplasmic binding proteins (PBP2) []. The PBP2 are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate- binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction [, , ]. |
