Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Acts in the intestine to regulate both innate immunity by promoting activation of PMK-1 and also stress response and life span by acting as an upstream, negative regulator of the daf-16 transcription factor. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domain 1 binds phorbol ester with low affinity. Phorbol-ester/DAG-type domain 2 binds phorbol ester with high affinity and targets the kinase to the cell periphery, enabling phosphorylation and activation by colocalized tpa-1. Both domains 1 and 2 appear to bind DAG with equal affinity so may contribute equally to translocation and activation. Translocation to the cell membrane is required for kinase activation. Expressed in the late embryo, all larval stages, and adult in the intestine and in cells positioned near the posterior bulb of the pharynx. Phosphorylation on Ser-925 by tpa-1 is the dominant regulator of catalysis, phosphorylation on Ser-929 by tpa-1 has a lesser effect. Prolonged phosphorylation results in ubiquitination and degradation. Increase in adult life span. Increased levels of daf-16 translocate into the nucleus in response to heat stress. Hypersensitive to killing by bacteria. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily.