The N-terminal domain (NTD) forms an outer membrane channel and is used for uptake of nutrients across the outer membrane. Also confers susceptibility to structurally different antibiotics and antituberculosis drugs, and to toxic immune factors such as nitric oxide (NO). The C-terminal domain (TNT) is dispensable for normal growth in macrophages. H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide Glycohydrolase activity is completely inhibited by interaction with the immunity factor for TNT (IFT) homolog. This inhibition protects M.bovis from self-poisoning. Interacts with the immunity factor for TNT (IFT) homolog. M.bovis does not permeabilize phagosomes and does not escape from phagosomes. Thus, the C-terminal TNT domain is likely trapped in phagosomes during M.bovis BCG infection, where it is incapable of inducing necrosis of macrophages. The C-terminal domain (TNT) is probably cleaved. Deletion of the gene confers high-level drug resistance to a wide range of antibiotics and antituberculosis drugs, and protects M.bovis from killing in macrophages that prevent intracellular mycobacterial replication. Increases resistance to small, hydrophilic antibiotics, to antituberculosis drugs, to large, hydrophobic or hydrophilic antibiotics such as erythromycin, rifampicin and streptomycin, and to nitric oxide. Under in vivo conditions, such as in human THP-1 macrophages, absence of the gene drastically reduces intracellular growth of M.bovis.