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Legionella pneumophila encodes an extracellular secreted phospholipase A named PlaA that is translocated by the type II secretion system. It plays an essential role in maintaining the integrity of Legionella‐containing vacuoles in L. pneumophila pathogenesis. Here, it is shown that PlaA has a main lysophospholipase activity to hydrolyze fatty‐acyl groups in lysophospholipids. Although it has a very low phospholipase A activity to catalyze the hydrolysis of fatty‐acyl groups in phospholipids, PlaA can bind phospholipids such as 1,2‐dipalmitoylphosphatidylcholine with a dissociation constant of 11.1 µM. Sequence‐alignment analysis combined with activity assays revealed that PlaA contains a distinct substrate‐binding site among the known structures of the phospholipase A family, implying that PlaA may present a novel mechanism for substrate recognition. Native PlaA and its selenomethionine (SeMet)‐substituted form were purified and crystallized by vapour diffusion in hanging drops at 296 K. Diffraction data were collected to a resolution of 2.0 Å for native PlaA protein and to a resolution of 2.7 Å for SeMet‐substituted PlaA protein. The crystals of native PlaA belonged to the monoclinic space group P21, while the crystals of SeMet‐substituted PlaA belonged to the primitive orthorhombic space group P212121. Initial phases for PlaA were obtained from SeMet SAD data sets. [ABSTRACT FROM AUTHOR]