v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry represents the substrate binding domainfound in the putative ABC transporter substrate-binding lipoprotein YvgL. It is a ModA-like protein that belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge [ ]. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap [].ModA proteins, which serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea [ ]. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate and tungstate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis []. |
| Short Name | YvgL-like_PBP2 |