{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Colautti J"],"funding":["U.S. Department of Energy","Institute of Infection and Immunity","Burroughs Wellcome Fund","Office of Science","Brookhaven National Laboratory","Canadian Institutes of Health Research"],"pagination":["110491"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12356396"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["301(8)"],"pubmed_abstract":["In metazoans, enzymes belonging to the bifunctional ADP-ribosyl cyclase/cyclic ADP-ribose (cADPr) hydrolase family regulate diverse cellular processes by synthesizing and hydrolyzing the intracellular second messenger cADPr, derived from the electron carrier NAD<sup>+</sup>. However, bacterial enzymes belonging to this family have not been characterized. Here, we identify a bacterial ADP-ribosyl cyclase that is associated with the type VII secretion system and functions as an antibacterial toxin. This enzyme, which we name Tac1, inhibits bacterial growth by rapidly hydrolyzing NAD<sup>+</sup> and NADP<sup>+</sup>. We determine the X-ray crystal structure of Tac1 to a resolution of 1.4 Å, which reveals that this protein adopts the core catalytic fold of metazoan ADP-ribosyl cyclase enzymes "],"journal":["The Journal of biological chemistry"],"pubmed_title":["Antibacterial ADP-ribosyl cyclase toxins inhibit bacterial growth by rapidly depleting NAD(P)<sup/>."],"pmcid":["PMC12356396"],"funding_grant_id":["DE-SC0012704","PJT-173486"],"pubmed_authors":["Kim Y","Colautti J","Whitney JC"],"additional_accession":[]},"is_claimable":false,"name":"Antibacterial ADP-ribosyl cyclase toxins inhibit bacterial growth by rapidly depleting NAD(P)<sup/>.","description":"In metazoans, enzymes belonging to the bifunctional ADP-ribosyl cyclase/cyclic ADP-ribose (cADPr) hydrolase family regulate diverse cellular processes by synthesizing and hydrolyzing the intracellular second messenger cADPr, derived from the electron carrier NAD<sup>+</sup>. However, bacterial enzymes belonging to this family have not been characterized. Here, we identify a bacterial ADP-ribosyl cyclase that is associated with the type VII secretion system and functions as an antibacterial toxin. This enzyme, which we name Tac1, inhibits bacterial growth by rapidly hydrolyzing NAD<sup>+</sup> and NADP<sup>+</sup>. We determine the X-ray crystal structure of Tac1 to a resolution of 1.4 Å, which reveals that this protein adopts the core catalytic fold of metazoan ADP-ribosyl cyclase enzymes ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-29T16:32:06.44Z","creation":"2026-04-08T05:25:01.263Z"},"accession":"S-EPMC12356396","cross_references":{"pubmed":["40680842"],"doi":["10.1016/j.jbc.2025.110491"]}}