Involved in proteolysis and elastolysis (degradation of the host protein elastin). Has staphylolytic activity (degrades pentaglycine cross-links in cell wall peptidogylcan), preferring Gly-Gly-|-X substrates where X is Ala or Gly (PubMed:11179971). Enhances the elastolytic but not proteolytic activity of elastase (lasB) and elastolytic activity of other proteases (PubMed:2110137). Degradation of host elastin is likely to contribute to the pathogenicity of P.aeruginosa. While either His-317 or His-356 can abstract a proton in the hydrolysis reaction, the same residue performs both functions in a given catalytic cycle, with the other stabilizing the catalytic intermediate (PubMed:20026068). Binds 1 zinc ion per subunit. kcat is 5.1 sec(-1), 5.3 sec(-1), 1.7 sec(-1) at pH 9, 8 and 7 respectively. Optimum pH is 8-9, inactive at pH 6 and below. Secreted in an Xcp-dependent fashion (a type II secretion pathway). Optimal protein expression in vivo requires both Zn(2+) and Ca(2+) during growth (at protein level). Processing of pro-LasA can occur extracellularly and requires elastase (lasB) (PubMed:9642203). Secretion and processing may be linked (PubMed:8932318). Loss of staphylolytic activity (lysis of heat-killed S.aureus). Belongs to the peptidase M23A family. Partial protein sequence was obtained following expression in E.coli, not P.aeruginosa. Truncated C-terminus. Truncated N-terminus.