CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D CBASS(GG) system (PubMed:32839535). The effector protein for this CBASS system. Binds c-di-GMP, does not bind cUMP-AMP (PubMed:32877915). Upon activation by c-di-GMP forms filaments which hydrolyze NAD(+); filament formation is required for enzyme activation (By similarity). H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide NAD(+) hydrolase activity is strongly stimulated by c-di-GMP, weakly by 3'3'-cGAMP, very weakly by c-di-AMP but not at all by 2'3'-cGAMP (Probable). Self-association of TIR domains is required for NADase activity (By similarity). The TIR domain mediates NAD(+) hydrolase (NADase) activity. The cyclic nucleotide binds in the C-terminal bacterial STING region. In the C-terminal section; belongs to the bacterial STING family.