Cholesterol-dependent cytolysins (CDCs) are bacterial pore-forming toxins that are secreted as soluble monomers and oligomerise into large circular pre-pores on the surface of cholesterol-rich membranes. Various structural changes and transitions results in insertion of β-hairpins into the lipid bilayer, forming a large β-barrel pore that results in cell lysis [1]. We have identified a highly conserved structural motif of CDCs that plays a critical role in the prepore-to-pore transition. Furthermore, this motif is also highly conserved in a large, diverse family of uncharacterised proteins from over 220 species, which we have designated the name “CDC-like” (CDCL) proteins [2]. Many of these CDCLs exist as homologous pairs. We have identified a novel CDCL pair, referred to as ALY long (ALYL) and ALY short (ALYS), that originates from the species Elizabethkingia anophelis, a commensal bacterium of the Anopheles mosquito. X-ray crystallography revealed the structure of monomeric ALYL consists of characteristic CDC domain 1 – 3 structure; however, domain 4 differs from that of CDCs significantly. In the presence of lipids, ALYL and ALYS show weak pore-forming activity and analysis by negative-staining electron microscopy reveals a large circular oligomeric complex reminiscent of CDC pore complexes. ALYS also forms a non-lytic circular oligomer in the absence of ALYL. XL-MS data reveals an initial insight into the structural changes between the monomeric and protomeric states, which will be further supported by the high-resolution cryo-EM structure of the complex. In summary, we have shown that the ALY toxins share some structural resemblance to CDCs, but form a two-component pore complex that is unique to the CDC family. This study establishes the beginning of an investigation into the large family of novel CDC-like proteins present in a wide range of bacterial species and are suspected to play key roles in microbial survival and human disease.