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(GG) CBASS system (PubMed:32839535). The effector protein for this CBASS system. Upon activation by c-di-GMP forms filaments which hydrolyze NAD(+); filament formation is required for enzyme activation. Induction in an E.coli strain that synthesizes c-di-GMP leads to significant growth inhibition. Binds c-di-GMP and 3'3'-cGAMP (3'3'-cyclic GMP-AMP), but not c-di-AMP, 2'3'-cGAMP or cUMP-AMP. 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 and not at all by 2'3'-cGAMP. Self-association of TIR domains is required for NADase activity. kcat is 2.3 sec(-1). Forms homodimers in equilibrium with homotetramers. In vitro, in the presence of c-di-GMP, forms filaments 25-30 nm in length with an ordered array of parallel-stacked homodimers. 3'3'-cGAMP weakly induces filament formation, while 2'3'-cGAMP does not. 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.