| Primary Identifier | IPR041879 | Type | Domain |
| Short Name | YvgL-like_PBP2 |
| 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 superfamilyof 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 []. |
