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Here, we report the structure of TfcB, comprising an N-terminal domain similar to the catalytic domain of glycosyl hydrolase (GH-19) chitinases and a C-terminal domain for recognition and translocation by the T4SS. Utilizing a two-hybrid assay to measure effector interactions with the T4SS coupling protein VirD4, we documented the existence of five more T4SS substrates. One of these was protein 20845, an annotated nuclease. A\n              <jats:italic>S. maltophilia<\/jats:italic>\n              mutant lacking the gene for 20845 was impaired for killing\n              <jats:italic>Escherichia coli<\/jats:italic>\n              ,\n              <jats:italic>Klebsiella pneumoniae<\/jats:italic>\n              , and\n              <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n              . Moreover, the cloned 20845 gene conferred robust toxicity, with the recombinant\n              <jats:italic>E. coli<\/jats:italic>\n              being rescued when 20845 was co-expressed with its cognate immunity protein. The 20845 effector was an 899 amino-acid protein, comprised of a GHH-nuclease domain in its N-terminus, a large central region of indeterminant function, and a C-terminus for secretion. Engineered variants of the 20845 gene that had mutations in the predicted catalytic site did not impede\n              <jats:italic>E. coli<\/jats:italic>\n              , indicating that the antibacterial effect of 20845 involves its nuclease activity. Using flow cytometry with DNA staining, we determined that 20845, but not its mutant variants, confers a loss in DNA content of target bacteria. Database searches revealed that uncharacterized homologs of 20845 occur within a range of bacteria. These data indicate that the\n              <jats:italic>S. maltophilia<\/jats:italic>\n              T4SS promotes interbacterial competition through the action of multiple toxic effectors, including a potent, novel DNase.\n            <\/jats:p>\n            <jats:sec>\n              <jats:title>IMPORTANCE<\/jats:title>\n              <jats:p>\n                <jats:italic>Stenotrophomonas maltophilia<\/jats:italic>\n                is a multi-drug-resistant, Gram-negative bacterium that is an emerging pathogen of humans. Patients with cystic fibrosis are particularly susceptible to\n                <jats:italic>S. maltophilia<\/jats:italic>\n                infection. In hospital water systems and various types of infections,\n                <jats:italic>S. maltophilia<\/jats:italic>\n                co-exists with other bacteria, including other pathogens such as\n                <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                . We previously demonstrated that\n                <jats:italic>S. maltophilia<\/jats:italic>\n                has a functional VirB\/D4 type VI protein secretion system (T4SS) that promotes contact-dependent killing of other bacteria. Since most work on antibacterial systems involves the type VI secretion system, this observation remains noteworthy. Moreover,\n                <jats:italic>S. maltophilia<\/jats:italic>\n                currently stands alone as a model for a human pathogen expressing an antibacterial T4SS. Using biochemical, genetic, and cell biological approaches, we now report both the discovery of a novel antibacterial nuclease (TfdA) and the first structural determination of a bactericidal T4SS effector (TfcB).\n              <\/jats:p>\n            <\/jats:sec>\n          <\/jats:sec>","DOI":"10.1128\/mbio.01198-24","type":"journal-article","created":{"date-parts":[[2024,6,4]],"date-time":"2024-06-04T13:50:21Z","timestamp":1717509021000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":9,"title":["Bactericidal effectors of the\n            <i>Stenotrophomonas maltophilia<\/i>\n            type IV secretion system: functional definition of the nuclease TfdA and structural determination of TfcB"],"prefix":"10.1128","volume":"15","author":[{"given":"Brandi L.","family":"Cobe","sequence":"first","affiliation":[{"name":"Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Supratim","family":"Dey","sequence":"additional","affiliation":[{"name":"Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Illinois, USA"},{"name":"Center for Structural Biology of Infectious Diseases, Northwestern University Feinberg School of Medicine, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"George","family":"Minasov","sequence":"additional","affiliation":[{"name":"Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Illinois, USA"},{"name":"Center for Structural Biology of Infectious Diseases, Northwestern University Feinberg School of Medicine, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1510-7412","authenticated-orcid":true,"given":"Nicole","family":"Inniss","sequence":"additional","affiliation":[{"name":"Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Illinois, USA"},{"name":"Center for Structural Biology of Infectious Diseases, Northwestern University Feinberg School of Medicine, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3274-7611","authenticated-orcid":true,"given":"Karla J. 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