Bacteria often interact with rival bacteria or with eukaryotic hosts and predators. All of these interactions can be affected by toxic proteins, called effectors, that are delivered directly into a neighboring cell by the bacterial type VI secretion system (T6SS). This contractile injection system shoots an effector-decorated, arrow-like structure out of the cell with great force; the arrow penetrates the neighboring cell and deploys the effectors inside it. Although many T6SS effector families have been identified, many still await discovery. I will discuss a new, widespread class of T6SS effectors that share an N-terminal domain named RIX. I will show that RIX targets proteins for secretion via T6SS, and that it is fused to polymorphic C-terminal domains that function as antibacterial toxins, anti-eukaryotic toxins, or as tethers for toxins encoded by other genes.