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In  Escherichia coli , formation of new cells is mediated by the elongasome and divisome that govern cell elongation and septation, respectively. Proper transition between these events is essential to ensure viable progeny are produced; however, the components of each complex responsible for transmission of the cell signal to shift from elongation to septation are unclear. Recently, a region within the N-terminal domain of the essential divisome protein FtsK (FtsK N ) was identified that points to a key role for FtsK as a checkpoint of cell envelope remodeling during division. Here, we used site-specific  in vivo  UV cross-linking to probe the periplasmic loops of FtsK N  for protein interaction partners critical for FtsK N  function. Mass spectrometry analysis of five unique FtsK N  periplasmic cross-links revealed a network of potential FtsK N  interactors, one of which included the septal peptidoglycan binding protein rare lipoprotein A (RlpA). This protein was further verified as a novel interaction partner of FtsK N  by an  in vitro  pull-down assay. Deletion of  rlpA  from an FtsK temperature-sensitive  E .  coli  strain partially restored cell growth and largely suppressed cellular filamentation compared to the wild-type strain. This suggests that interaction with RlpA may be critical in suppressing septation until proper assembly of the divisome.

Outer membrane lipoprotein RlpA is a novel periplasmic interaction partner of the cell division protein FtsK in Escherichia coli