FIG 7 .
Organization of P. acnes phage endolysins. (A) Organization of the P. acnes endolysins and their closest homologues present in Rhodococcus phages ReqiDocB7 and REQ2 and a group of subcluster B1 mycobacteriophages of which KLucky39 is representative. All have an amidase-2 domain that cleaves peptidoglycan but have different and unrelated C-terminal domains, which are presumed to confer cell wall binding specificity. The KLucky39 endolysin—like many of the mycobacteriophage endolysins—contains three domains, including an N-terminal M23 peptidase (26). (B) Alignment of the P. acnes phage endolysins shows that they are closely related and display the greatest amino acid sequence differences at around position 200, which likely corresponds to a glycine-rich interdomain linker.