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The hydrolysis of septal PG (sPG) is a crucial step of bacterial cell division, facilitated by FtsEX through an amidase activation system. In this study, we present the cryo-EM structures of <jats:italic>Escherichia coli<\/jats:italic> FtsEX and FtsEX-EnvC in the ATP-bound state at resolutions of 3.05 \u00c5 and 3.11 \u00c5, respectively. Our PG degradation assays in <jats:italic>E<\/jats:italic>. <jats:italic>coli<\/jats:italic> reveal that the ATP-bound conformation of FtsEX activates sPG hydrolysis of EnvC-AmiB, whereas EnvC-AmiB alone exhibits autoinhibition. Structural analyses indicate that ATP binding induces conformational changes in FtsEX-EnvC, leading to significant differences from the apo state. Furthermore, PG degradation assays of AmiB mutants confirm that the regulation of AmiB by FtsEX-EnvC is achieved through the interaction between EnvC-AmiB. 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