Probable protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing either m-Dpm (meso-diaminopimelate) or L-lys, which act as spore germinants. Probably autophosphorylates and phosphorylates FusA (EF-G, elongation factor G); the latter modification is likely necessary for germination in response to peptidoglycan. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Homodimer. Is associated with the inner membrane of the spore. The C-terminal extracellular domain containing the PASTA repeats binds peptidoglycan. PubMed:18984160 shows that peptidoglycan fragments serve as a novel mechanism of interspecies bacterial signaling that likely indicates the presence of growing bacteria and thus serve as a signal for dormant cells that growth-promoting conditions exist. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.