A phosphodiesterase (PDE) that hydrolyzes cyclic di-3',5'-adenylate (c-di-AMP); there are at least 2 PDEs for c-di-AMP in this bacteria (this and pdeA), this may be the major PDE for growth in liquid culture (PubMed:25583510). During host infection c-di-AMP is secreted into the host cytoplasm which leads to interferon-beta production and secretion by the host (Probable). The cytoplasmic HD domain binds and hydrolyzes c-di-AMP to 5'-pApA; has very low activity against c-di-GMP, does not hydrolyze ppGpp (PubMed:25583510). 3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H(+) Able to bind Fe(2+), but has only very weak PDE activity. c-di-AMP hydrolysis inhibited by ppGpp, without altering c-di-AMP binding. The cytoplasmic domain (residues 494-718, expressed as a maltose-binding protein fusion) has c-di-AMP phosphodiesterase activity. Grows as well as wild-type in culture and in macrophages, double pdeA-pgpH mutants have slightly defective growth in culture and in macrophages. Single mutant secretes 2-fold more c-di-AMP, double mutant secretes about 4-fold more. Single mutant induces wild-type interferon-beta (IFN-beta) transcription by macrophages, double pdeA-pgpH mutants induces about 10-fold more IFN-beta. Double mutant is 10(3)-fold less virulent in mice, suggesting increased bacterial c-di-AMP is detrimental to growth within the host. Belongs to the PgpH phosphodiesterase family.