Eimeria tenella is a deadly and contagious apicomplexan protozoan parasite, which is responsible for avian coccidiosis. This pathology induces major economic losses for poultry industry worldwide. E. tenella invades the digestive epithelial cells, causing intestinal lesions that can lead to death. Coccidiostatic drugs and vaccination are necessary to control coccidiosis. However, with the apparition of resistance against anticoccidian molecules in parasite field strains and the high cost of vaccines, it appears necessary to improve the means of control of this parasite. Our research is focused on the understanding of E. tenella rhoptry protein kinase (ROPK) functions. It is well known that invasion of apicomplexan parasite is orchestrated by protein secretion. Among the proteins secreted, ROPKs are well described in Toxoplasma gondii as key virulence factors. ROPKs are involved in the modulation of numerous cellular functions and pathways allowing parasite development. The knowledge about the functions of E. tenella ROPK is limited. E. tenella kinome is predicted to contain 28 putative ROP kinases. Among them, two predicted kinases were identified in the rhoptry proteome of E. tenella sporozoites. In this context, our research is focused on understanding the mode of action of E. tenella ROPK. We previously established that the first kinase, EtROP1, is active and phosphorylates the cellular p53, inhibiting the apoptosis of parasited cells and thus promoting the parasite development. The second kinase, EtROP2, is an active kinase localized in the rhoptry compartment and is early expressed during the parasite life cycle. Interestingly, we show that the overexpression of EtROP2 could speed up the parasitic life cycle, favoring the excretion of oocysts 1-2 days earlier than a wild-type strain. Understanding the role of EtROP2 in the host-parasite interaction may reveal this kinase as a good candidate in the race of improvement of the means of control for coccidiosis.