In order to characterize the role of CglE in the pathogenesis of Escherichia coli K1 meningitis, comparative infectomic approaches were used to analyze and predict its functions. CglE and IbeA are present in GimA as a pair of homologous proteins at different locations. A similar pair of proteins is also present in Silicibacter sp which belongs to the most abundant marine bacterial groups. Both bacteria have to survive under harsh environments (cerebrospinal fluid and ocean) with poor nutrition, suggesting that they are important for energy metabolism in the both microbes. The bioinformatic analysis indicated that CglE is a putative dihydrolipoamide dehydrogenase, and also shares 55% protein sequence identity to IbeA. The hydrophilicity and antigenic index between them are very similar. Molecular approaches were further used to determine whether CglE shares similar functions as IbeA. The results showed that CglE was able to bind to vimentin, an IbeA-binding protein. The biological functions of CglE need to be further examined.