A gene encoding an extracellular lipase was identified in Staphylococcus warneri 863. The deduced lipase is organised as a prepro-protein and has significant similarity to other staphylococcal lipases. The mature part of the lipase was expressed with an N-terminal histidine tag in Escherichia coli, purified and biochemically characterised. The results show that the purified lipase (named SWL2) combines the properties of the staphylococcal lipases characterised so far. It has both a high preference for short chain substrates and surprisingly, it also displays phospholipase activity. Homology alignment was used to analyse sequence-function relationships of the staphylococcal lipase family with the aim to identify the structural basis underlying the different properties of the staphylococcal lipases.