BacA is a bacterial lysin from Enterococcus faecalis that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. BacA is homologous to the YbfG and YkuG lysins of Bacillus subtilis. BacA has a C-terminal catalytic glycosyl hydrolase family 25 (GH25) domain and an N-terminal peptidoglycan-binding domain comprised of three alpha helices which is similar to a domain found in matrixins.