The type VI secretion system (T6SS) is a unique molecular machine found in many Gram‑negative bacteria that delivers protein “effectors” directly into other cells. Effectors are delivered through interactions with Hcp, PAAR, and VgrG proteins. Acinetobacter baumannii AB307‑0294 delivers three antibacterial effectors via the T6SS through direct interaction with three cognate VgrG tip proteins and encodes two PAAR proteins without cognate effectors. Both paar genes were deleted via homologous recombination, individually and together. Loss of either PAAR protein from A. baumannii alone did not result in altered T6SS activity. However, loss of both PAAR proteins resulted in complete abrogation of T6SS activity. Complementation of the double paar mutant strain with PAAR2 completely restored T6SS activity, including delivery of all effector proteins, while complementation with PAAR1 partially restored T6SS activity. Examination of the architecture of PAAR2 protein revealed a predicted PAAR domain within the N‑terminal region; no known domains were identified in the remainder of the protein. To assess the functional importance of the N-terminal region, we made a mutation approximately 303 bases into the paar2, leaving the PAAR domain of the encoded protein intact. This mutation alone, or combined with a paar1 mutation, did not result in altered T6SS function. Furthermore, complementation of the double paar mutant with the first 101 amino acids of PAAR2 (containing the PAAR domain) resulted in full restoration of T6SS function and delivery of all effectors. Together, these results suggest that the A. baumannii PAAR proteins are functionally redundant; however, at least one protein is essential for activity of the T6SS. Understanding the role that PAAR proteins play in the delivery of A. baumannii T6SS effectors is critical to our understanding of this unique molecular weapon.