Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions. Binds 1 zinc ion per subunit. Protease activity is inhibited by the metal chelating reagents 1,10-phenanthroline and EDTA. Interacts with BamA and LoiP. A significant amount of BepA is membrane-associated. This localization could result from interaction with the BAM complex. Disruption sensitizes cells to multiple drugs. Belongs to the peptidase M48 family. BepA subfamily.