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An overlooked reservoir of antimicrobials lies in the form of PG-hydrolyzing enzymes naturally produced for polymicrobial competition, particularly those associated with the type VI secretion system (T6SS). Here, we report that a T6SS effector TseP, from\n                    <jats:italic>Aeromonas dhakensis<\/jats:italic>\n                    , represents a family of effectors with dual amidase-lysozyme activities. In vitro PG-digestion coupled with LC-MS analysis revealed the N-domain\u2019s amidase activity, which is neutralized by either catalytic mutations or the presence of the immunity protein TsiP. The N-domain, but not the C-domain, of TseP is sufficient to restore T6SS secretion in T6SS-defective mutants, underscoring its critical structural role. Using pull-down and secretion assays, we showed that these two domains interact directly with a carrier protein VgrG2 and can be secreted separately. Homologs in\n                    <jats:italic>Aeromonas hydrophila<\/jats:italic>\n                    and\n                    <jats:italic>Pseudomonas syringae<\/jats:italic>\n                    exhibited analogous dual functions. Additionally, N- and C-domains display distinctive GC contents, suggesting an evolutionary fusion event. By altering the surface charge through structural-guided design, we engineered the TseP\n                    <jats:sup>C4+<\/jats:sup>\n                    effector that successfully lyses otherwise resistant\n                    <jats:italic>Bacillus subtilis<\/jats:italic>\n                    cells, enabling the T6SS to inhibit\n                    <jats:italic>B. subtilis<\/jats:italic>\n                    in a contact-independent manner. This research uncovers TseP as a new family of bifunctional chimeric effectors targeting PG, offering a potential strategy to harness these proteins in the fight against antimicrobial resistance.\n                  <\/jats:p>","DOI":"10.7554\/elife.101125","type":"journal-article","created":{"date-parts":[[2024,10,15]],"date-time":"2024-10-15T14:25:22Z","timestamp":1729002322000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.101125","source":"Crossref","is-referenced-by-count":6,"title":["Amidase and lysozyme dual functions in TseP reveal a new family of chimeric effectors in the type VI secretion system"],"prefix":"10.7554","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-0532-1070","authenticated-orcid":true,"given":"Zeng-Hang","family":"Wang","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0220qvk04","id-type":"ROR","asserted-by":"publisher"}],"name":"State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of 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