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Also binds c-diAMP or linear di-AMP with lower affinity. The nuclease digests dsDNA to about 50 bp lengths with a 2-base 3' overhang and a consensus recognition site of 5'-Axx|T-3'. DNA has been modeled to contact a pair of juxtaposed active sites (one from each layer of the hexamer), accounting for cleavage on both strands and the 2-base overhang (PubMed:31932164)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31932164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31932165"}],"value":"Protects E.coli strain JP313 against bacteriophage lambda cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into a susceptible strain it confers bacteriophage immunity. Mutations in the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC) but not the disassembly protein (Cap6 also called Trip13) no longer confer immunity. The presence of the intact operon leads to culture collapse and cell death which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31932164"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6P7O"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31932164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31932165"}],"value":"Activated by cAAA and to a lesser extent cAA and cAAG; cAAA and cAA are products of its cognate CD-NTase. Cyclic nucleotide binding causes hexamerization (PubMed:31932165). Cyclic nucleotide binding causes a series of shifts that enclose the cAAA molecule, enable hexamer formation and juxtapose pairs of active sites to allow dsDNA cleavage (PubMed:31932164)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31932164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31932165"}],"value":"Self-oligomerizes (PubMed:31932165). Forms homotrimers; in the presence of cAAA the trimers associate face-to-face to form homohexamers. 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