Outer membrane phospholipase A1 (OMPLA) is an acyl hydrolase with a broad substrate specificity (EC:3.1.1.32.)

It has been proposed that Ser164 is the active site of the protein (UniProt P00631) [1] This integral membrane phospholipase was found in many Gram-negative bacteria and has a broad substrate specificity EC 3.1.1.32.

[2] The reaction products enhance the permeability of the outer membrane, which allows the semispecific secretion of bacteriocins.

One speculative function of OMPLA is related to organic solvent tolerance in bacteria.

The active site His and Ser residues are located at the exterior of the beta-barrel, at the outer leaflet side of the membrane.