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Summary  Proteolytic control of   C   aulobacter  cell cycle proteins is primarily executed by  ClpXP , a dynamically localized protease implicated in turnover of several factors critical for faithful cell cycle progression. Here, we show that the transient midcell localization of  ClpXP  that precedes cytokinesis requires the  FtsZ  component of the divisome. Although  ClpAP  does not exhibit subcellular localization,  FtsZ  is a substrate of both  ClpXP  and  ClpAP   in vivo  and  in vitro . A peptide containing the  C ‐terminal portion of the  FtsA  divisome protein is a substrate of both  ClpXP  and  ClpAP   in vitro  but is primarily degraded by  ClpAP   in vivo .   C   aulobacter  carries out an asymmetric division in which  FtsZ  and  FtsA  are stable in stalked cells but degraded in the non‐replicative swarmer cell where  ClpAP  alone degrades  FtsA  and both  ClpAP  and  ClpXP  degrade  FtsZ . While asymmetric division in   C   aulobacter  normally yields larger stalked and smaller swarmer daughters, we observe a loss of asymmetric size distribution among daughter cells when   clpA   is depleted from a strain in which  FtsZ  is constitutively produced. Taken together, these results suggest that the activity of both  ClpXP  and  ClpAP  on divisome substrates is differentially regulated in daughter cells.

ClpXP and ClpAP proteolytic activity on divisome substrates is differentially regulated following the C aulobacter asymmetric cell division