Catalyzes the formation of the second messenger cAMP. ATP = 3',5'-cyclic AMP + diphosphate The isolated catalytic domain prefers Mn(2+) over Mg(2+) as a cofactor. At pH 6.0. Optimum pH is 6.0. Homodimer. A possible member of the dormancy regulon. Induced in response to reduced oxygen tension (hypoxia). It is hoped that this regulon will give insight into the latent, or dormant phase of infection. Consists of 3 structural domains. The pH-responsive N-terminus inhibits the adenylyl cyclase (AC) activity of the C-terminal catalytic domain. The length of the linker segment (aa 192-206) is decisive for regulation. No visible phenotype following infection of SPF C57BL/6 mice. Was identified as a high-confidence drug target. Binds 1 C18:1 fatty acid per monomer. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.