Part of the H2 type VI secretion system (H2-T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (PubMed:26037124, PubMed:31577948, PubMed:31231326). Forms the spike at the tip of the elongating tube probably formed by haemolysin co-regulated protein 2b/Hcp2b (Probable). Allows the delivery of the Tle3 antibacterial toxin to target cells where it exerts its toxicity (PubMed:31231326). Additionally, acts directly as an effector and promotes internalization by interacting with the host gamma-tubulin ring complex (PubMed:26037124). Elicits toxicity also in the bacterial periplasm and disrupts bacterial cell morphology. Toxicity is counteracted by a cognate immunity protein (PubMed:31577948). Interacts with Tla3; this interaction promotes Tle3 loading onto VgrG2b. Interacts with host gamma-tubulin ring complex components GCP1 and GCP4. Secreted by the H2 type VI (H2-T6SS) secretion system involving VgrG2a into host cells upon infection. The C-terminal region is part of a wide family of metallopeptidase effectors. Deletion leads to a 75% loss of internalization of P.aeruginosa into host cell. Belongs to the VgrG protein family.