Escherichia coli (Ec) has been used to study the function of cell division proteins from different microorganisms, especially when genetic tools are limited for studying these proteins in their native hosts. The expression of ftsA from Neisseria gonorrhoeae (Ng) disrupted cell division in E. coli resulting in a significant increase in cell length. In some cells, FtsANg localised to the division site and the poles of E. coli cells, but the majority of cells showed no specifical localisation. FtsANg did not complement an E. coli ftsA mutant strain. Bacterial two-hybrid and GST pull-down assays indicated that FtsANg interacted with FtsNEc, but no other cell division proteins from E. coli. This interaction was mediated through the 2A and 2B subdomains of FtsANg. This evidence suggests that the function of FtsANg is species specific.