The Staphylococcus aureus pathogenicity islands (SaPIs) are phage-inducible chromosomal islands (PICI) that are widely spread among the staphylococci as mobile genetic elements (Penades & Christie, 2015). The SaPIs play significant role in the Staphylococci pathogenicity due to they are carry and disseminate superantigen genes, especially those for toxic shock toxin and enterotoxin B (Novick et al., 2010). In nature, SaPIs are integrated to the Staphylococcus aureus chromosome passively under the control of a master repressor Stl, a DNA binding protein (Úbeda et al., 2008). Accordingly, following infection of SaPIs positive strains by a helper phage, SaPIs excise, replicate and are packaged in phage-like particles composed of phage virion proteins. Our previous work indicated that SaPI de-repression is effected by specific, non-essential phage proteins that bind to Stl, disrupting the Stl-DNA complex and thereby initiating the excision-replication-packaging (ERP) cycle of the islands. Different SaPIs encode different Stl repressors, so each SaPI requires a different non-essential phage protein for its de-repression (Tormo-Mas et al., 2010). Here, and for the first time, we have identified an essential phage protein involved in the de-repression of SaPI2, the phage 80α recombinase sak. Not only this, but also two non-related recombinases from phages 52A and SLT are capable of de-repressing SaPI2. The fact that the Stl repressors interact with structurally unrelated proteins performing the same function make this strategy unique in nature and extremely effective. This highlights SaPIs as one of the most fascinating and effective subcellular parasites.