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While most strains encode three T6SSs, additional T6SS clusters have been identified in clinical isolates through comparative genomics, but their functions and effector biology remain undefined. Here, we identify TseMt as a major antibacterial effector associated with an H4\u2010T6SS in a clinical\n                    <jats:italic>P. aeruginosa<\/jats:italic>\n                    isolate LYSZa7. TseMt is a periplasmically active toxin whose activity is neutralized by a cognate immunity protein, TsiMt. Biochemical assays show that TseMt binds membranes and forms ion\u2010conducting pores, establishing it as a pore\u2010forming effector. A 3.0\u2009\u00c5 cryo\u2010electron microscopy structure reveals a distinct three\u2010domain architecture comprising an N\u2010terminal MIX\u2010like domain, a central \u03b1\u2010helical scaffold, and a C\u2010terminal toxin domain. Genetic analysis and structural modeling indicate that TseMt is delivered through a dedicated PAAR\u2212VgrG\u2212chaperone pathway. Together, these findings define the structural basis, functional mechanism, and delivery pathway of the H4\u2010T6SS effector TseMt from a clinical\n                    <jats:italic>P. aeruginosa<\/jats:italic>\n                    isolate and reveal its role in mediating bacterial competition.\n                  <\/jats:p>","DOI":"10.1002\/mlf2.70108","type":"journal-article","created":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T11:07:15Z","timestamp":1787828835000},"page":"417-431","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Functional characterization of a pore\u2010forming effector TseMt from the H4 type VI secretion system of\n                    <i>Pseudomonas aeruginosa<\/i>"],"prefix":"10.1002","volume":"5","author":[{"given":"Liwen","family":"Wu","sequence":"first","affiliation":[{"name":"Department of Immunology and Microbiology School of Life Sciences, Guangming Advanced Research Institute, 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