1.C.1.3.6
Colicin-like pore-forming domain protein, PmnH, of 462 aas and 2 C-terminal TMSs.  This protein has a dual-toxin architecture, having both an N-terminal colicin M-like domain, potentially interfering with peptidoglycan synthesis, and a colicin N-type domain, a pore-forming module distinct from the colicin Ia-type domain in Pseudomonas aeruginosa pyocin S5 (Ghequire et al. 2017).  Enhanced killing activity of PmnH under iron-limited growth conditions is due to parasitism of the ferrichrome-type transporter for entry into target cells, a strategy shown here to be used as well by monodomain colicin M-like bacteriocins from pseudomonads (Ghequire et al. 2017).