| Primary Identifier | IPR037420 | Type | Domain |
| Short Name | AmpR_PBP2 |
| description | This entry represents the C-terminal substrate binding domain of LysR-type transcriptional regulator AmpR, whichis involved in control of the expression of beta-lactamase genes []. Beta-lactamases are responsible for bacterial resistance to beta-lactam antibiotics such as penicillins. AmpR regulates the expression of beta-lactamases in many enterobacterial strains and many other Gram-negative bacilli. AmpR is a key player in the intricate network of regulators that is responsible for mediating virulence and antibiotic resistance in P. aeruginosa []. The topology of this substrate-binding domain is most similar to that of 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 [, , ]. |
