Antimicrobial peptide that acts against Gram-positive bacteria (Listeria spp., Enterococcus spp., B.subtilis, B.anthracis, P.aeruginosa) (PubMed:25342741, PubMed:28825809). Is not active against Gram-negative bacteria (PubMed:25342741). It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio), probably anchoring lipid II to the membrane, thus inhibiting cell wall synthesis (PubMed:25342741, PubMed:28825809). The interaction with lipid II involves the third position of the pentapeptide (PubMed:25342741). Shows bactericidal activity at about 2-fold minimal inhibitory concentrations (MIC), but does not form pore across the membrane (PubMed:25342741). Optimum pH is 1-8. Optimum temperature is 4-90 degrees Celsius. specific localization at active cell wall synthesis sites. Contains a unique connectivity of 6 cysteine bonds in contrast to most other CS-alpha-beta defensins which are linked by 3 or 4 disulfide bonds. Disulfide bonds are essential for structural integrity and antibacterial activity, since activity is lost after treatment with reducing agents. Thanks to disulfide bonds and N-terminal pyroglutamate, the protein is extremely stable in a wide pH and temperature range and insensitive toward proteases. Belongs to the invertebrate defensin family.