v5.1.0.3
Glycine data from LIS
Type | Family |
Description | Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. The protein components of these traffic systems include one or two transmembrane protein components, one or two membrane-associated ATP-binding proteins and a high affinity periplasmic solute-binding protein. In Gram-positive bacteria, which are surrounded by a single membrane and therefore have no periplasmic region, the equivalent proteins are bound to the membrane via an N-terminal lipid anchor. These homologue proteins do not play an integral role in the transport process per se, but probably serve as receptors to trigger or initiate translocation of the solute through the membrane by binding to external sites of the integral membrane proteins of the efflux system. In addition at least some solute-binding proteins function in the initiation of sensory transduction pathways.The bacterial Spermidine/putrescine-binding periplasmic protein (PotD) is involved in the polyamine transport system. It is required for the activity of the bacterialperiplasmic transport system of putrescine and spermidine [ , ]. This protein has two domains connected throughtwo β-strands, which form a hinge at the bottom of the central cleft, and this hinge lies and one short peptide segment [].Similar proteins with specificities for putrecine and spermidine are also included in this family, such as Putrescine-binding periplasmic protein PotF from Escherichia coli, more specifically involved in putrescine uptake [ , , ] and Spermidine-binding periplasmic protein SpuE from Pseudomonas aeruginosa [] respectively.Putrescine/cadaverine-binding protein and Putrescine/agmatine-binding protein from P. aeruginosa also belong to this entry [ ]. |
Short Name | Sperm_putr-bd |