Bacillus cereus is a ubiquitous, spore-forming bacterium and an opportunistic human pathogen responsible for diarrheal and emetic types of food poisoning. In order to control and prevent B. cereus food poisoning, we isolated a bacteriophage PBC2 from sewage and characterized its endolysin LysPBC2. The bacteriophage PBC2 belongs to the Siphoviridae family and has a very long flexible and non-contractile tail. While PBC2 phage has very narrow host range, the endolysin of phage PBC2, LysPBC2, and its catalytic domain showed broader lytic spectrum in that they could lyse Bacillus subtilis, Listeria monocytogenes, and Clostridium perfringens as well as the B. cereus group strains tested. However, the binding range of green fluorescent protein-fused cell wall binding domain (CBD) of LysPBC2 was limited to the bacteria in the B. cereus group. Interestingly, LysPBC2 has a spore binding domain (SBD) partially overlapped with its catalytic domain, which specifically binds to B. cereus spores but not to vegetative forms of B. cereus. Both transmission electron microscopy and fluorescence data suggest that the spore coat is the most probable binding target of the SBD suggesting a possible influence of endolysin in germination process. Furthermore, the versatile domains of LysPBC2 could be useful for developing more efficient biocontrol and detection agents against B. cereus.