Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (target cell counts decrease about 10,0000-fold for this system). CdiA toxicity is neutralized by its cognate immunity protein CdiI-NC101, but not by CdiI from other bacteria (PubMed:26305955, PubMed:28973472). The C-terminal domain (CT) cleaves tRNA endonucleolytically at the 5' side of guanine discriminator nucleotide sites (removes the last 4 nucleotides of the tRNA acceptor arm when the first nucleotide to be removed is G) (PubMed:28973472). Requires EF-Ts (tsf) for toxic function of the CT domain in vivo (PubMed:28223500). In vitro the CT tRNase activity requires both EF-Tu (tufA) and EF-Ts. EF-Ts probably increases steady-state GTP-EF-Tu-aa-tRNA substrate levels. The CT domain is thought to remodel this same complex to displace the 3'-end of the aa-tRNA and allow it to enter into the toxin active site (PubMed:28973472). The CT domain gains access to the cytoplasm of target cells by using integral inner membrane protein PTS system glucose-specific EIICB component (ptsG) (PubMed:26305955). The CdiA protein is thought to be exported from the cell through the central lumen of CdiB, the other half of its two-partner system (TPS). The TPS domain probably remains associated with CdiB while the FHA-1 domain forms an extended filament with the receptor-binding domain (RBD) at its extremity; in the secretion arrested state the C-terminus of the RBD and YP domains form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. The YP domain is probably responsible for this arrest at the point where it re-enters the host cell periplasm. Upon binding to a target cell outer membrane receptor a signal is transmitted to activate secretion. The filament elongates slightly, the rest of CdiA is secreted and the FHA-2 domain becomes stably associated with the target cell's outer membrane where it facilitates entry of the toxic CT domain into the target cell periplasm. From there the toxic CT domain is cleaved and gains access to the target cell cytoplasm via an inner membrane protein (PtsG for this CDI). Forms a contact-dependent growth inhibition complex of CdiA-CT-NC101, CdiI-NC101 and EF-Tu; the complex is a dimer of heterotrimers. Stable CdiA-CT-NC101, EF-Tu complexes are not detected, nor are complexes with EF-Ts. Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner. The C-terminal domain (CT) has toxic tRNase activity. In the N-terminal section; belongs to the CdiA toxin family.