Malaria is a global threat which is caused by a parasite of the genus Plasmodium, with P. falciparum being the most lethal strain. Anti-malarial drugs which have been developed are not necessarily effective due to this parasite’s acquired resistance to the drugs. Understanding protein homeostasis may aid in drug development against malaria especially when the homeostasis occurs in an organelle unique to the parasite: the apicoplast. The apicoplast is unique to the parasite and it houses proteases which regulate protein homeostasis. These proteases are conserved through evolution and thus, bacterial orthologues do exist in the eukaryote P. falciparum. ClpAP is one of the chaperone-proteases which exist in bacteria and it is categorized under the AAA+ family. This protease requires an adaptor protein, ClpS, to recognize N-degrons, which are protein substrates harbouring a primary destabilizing residue at its N-domain. Recently, a putative ClpS orthologue was discovered in P. falciparum (PfClpS) and it was speculated that it functions in a similar manner to that of bacterial ClpS. In this study, it is of interest to not only depict the interaction between PfClpS and bacterial N-degron substrates, but also its ability to dock onto bacterial ClpAP. From the degradation assays, it was shown that PfClpS is likely to recognize bacterial N-degron substrates but it does not interact with ClpAP. Interestingly, it was also shown that PfClpS could possibly interact with eukaryotic N-degron substrates. This discovery helps in the understanding of protein quality control in P. falciparum, which could not only be beneficial in future drug development, but also in understanding the mechanism of N-degron recognition in eukaryotes.