Pre-vacuolar protein sorting protein involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex. Required for extracellular secretion of the secreted aspartyl proteases SAP2, SAP4, SAP5, and SAP6. Its regulation of the pre-vacuolar secretory pathway is critical for virulence. Monomer or homodimer (in nucleotide-free form). Decamer, dodecamer or tetradecamer of two stacked respective homooligomeric rings (when bound to ATP); the dodecameric form seems to be predominant. Expression is regulated by GCN2 and GCN4. Leads to defects in endocytosis. Displays a characteristic class E vacuolar morphology and multilamellar structures consistent with an aberrant prevacuolar compartment. Missorts several vacuolar proteins to the extracellular space, including carboxypeptidase (CPY), vacuolar protease A (PrA), and vacuolar protease B (PrB). In addition, certain soluble secretory proteins, such as invertase and acid phosphatase, are missorted from the pre-vacuolar compartment (PVC) to the general secretory pathway prior to exocytosis. Results also in a decrease of canonically secreted proteins. Shows increased biofilm formation. Causes reduced tissue damage in an in vitro oral epithelial model (OEM) of tissue invasion, and defects in macrophage killing in vitro. Shows also attenuated virulence in an in vivo Caenorhabditis elegans model representative of intestinal epithelial infection. Belongs to the AAA ATPase family.