In Escherichia coli the divisome consists of 10 essential proteins, and is responsible for septum formation, constriction of membranes, and synthesis of septal peptidoglycan. The divisome protein FtsK is an integral-membrane protein that is implicated in cell division and chromosome segregation. The N-terminal portion of FtsK (FtsKN) is the only domain required for cell division. This project provides insight into the tertiary structure of FtsKN using covariance-guided structural modelling in combination with in vivo functional assays. GREMLIN was used to predict amino acids in contact within FtsKN and allowed for the generation of preliminary in silico models. Contact predictions were tested via temperature-sensitive complementation assays assessing cell morphology and length. The in vivo testing identified residues pairs believed to be in contact within the tertiary structure of FtsKN, and highlights areas of importance for future studies.