Lactic acid bacteria produce several types of pore forming peptides. Class I bacteriocins are lantibiotics that contain (methyl)lanthionine residues that may form intramolecular thioether rings. These peptides generally have a broad spectrum of activity and form unstable pores. Class II bacteriocins are small, heat stable peptides mostly with a narrow spectrum of activity. Most bacteriocins interact with anionic lipids that are abundantly present in the membranes of gram-positive bacteria. 'Docking molecules' may enhance the conductivity and stability of lantibiotic pores, while 'receptors' in the target membrane may determine specificity of class II bacteriocins. Insertion into the membrane of many bacteriocins is proton motive force driven. Lantibiotics may form pores according to a 'wedge-like' model, while class II bacteriocins may enhance membrane permeability either by the formation of a 'barrel stave' pore or by a 'carpet' mechanism.