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Significance The type VI secretion system (T6SS) is a molecular weapon used for interbacterial competition. It acts like a crossbow bolt to deliver toxic effectors into target cells. Here we characterize a T6SS toxin which we call Tse7. We show that it is a DNase and that its two-domain PAAR-nuclease structure allows coupling to the T6SS VgrG tip via the PAAR domain. Disruption of this interface abrogates toxin delivery and results in the loss of interbacterial killing ability. We identify the corresponding immunity protein, Tsi7, and show it directly interacts with the Tse7 toxin. Finally, as Tse7–Tsi7 sequences vary significantly betweenPseudomonas aeruginosa strains, and as Tsi7 protection is strain specific, we show that this toxin/immunity pair contributes to self- nonself-recognition.

The Pseudomonas aeruginosa T6SS-VgrG1b spike is topped by a PAAR protein eliciting DNA damage to bacterial competitors