Shows weak antimicrobial activity against its phylogenetic relative Caulobacter crescentus. Does not show activity against other bacteria tested (E.coli, Vibrio sp, Burkhoderia thailandensis, and Salmonella newport). Irreversibly unfolds upon heat treatment (PubMed:23601645). Between 50 and 65 degrees Celsius, the protein shows an intermediate fold (PubMed:23601645). At more than 65 degrees Celsius, the protein is completely unfolded (PubMed:23601645). Is composed of a ring composed by 9 residues, a loop and a C-terminal tail (PubMed:23601645). The peptide is threaded when the C-terminal tail is inserted throught the isopeptide-bonded ring (Probable). This lasso peptide is probably hydrolyzed to a linear form by the isopeptidase AtxE1, in vivo. when expressed in E.coli.