biostudies-literatureViola MGBrown UniversityNational Science Foundation of Sri LankaNational Institute of General Medical SciencesNIGMS NIH HHSe4306https://www.ebi.ac.uk/biostudies/studies/S-EPMC8996474biostudies-literatureUnknown31(5)The essential bacterial division protein in Escherichia coli, FtsZ, assembles into the FtsZ-ring at midcell and recruits other proteins to the division site to promote septation. A region of the FtsZ amino acid sequence that links the conserved polymerization domain to a C-terminal protein interaction site was predicted to be intrinsically disordered and has been implicated in modulating spacing and architectural arrangements of FtsZ filaments. While the majority of cell division proteins that directly bind to FtsZ engage either the polymerization domain or the C-terminal interaction site, ClpX, the recognition and unfolding component of the bacterial ClpXP proteasome, has a secondary interaction with the predicted intrinsically disordered region (IDR) of FtsZ when FtsZ is polymerized. HerProtein science : a publication of the Protein SocietyAn enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease.PMC8996474T32 GM07601R01GM1189271845734R01 GM118927Viola MGLaBreck CJCamberg JLPena CMXuan BFawzi NLRahmani NChua XYMathews KLPerdikari TMTrebino CEfalseAn enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease.The essential bacterial division protein in Escherichia coli, FtsZ, assembles into the FtsZ-ring at midcell and recruits other proteins to the division site to promote septation. A region of the FtsZ amino acid sequence that links the conserved polymerization domain to a C-terminal protein interaction site was predicted to be intrinsically disordered and has been implicated in modulating spacing and architectural arrangements of FtsZ filaments. While the majority of cell division proteins that directly bind to FtsZ engage either the polymerization domain or the C-terminal interaction site, ClpX, the recognition and unfolding component of the bacterial ClpXP proteasome, has a secondary interaction with the predicted intrinsically disordered region (IDR) of FtsZ when FtsZ is polymerized. Her2022-01-01T00:00:00Z2022 May2025-04-27T04:16:27.176Z2025-04-06T19:09:36.926ZS-EPMC89964743548164810.1002/pro.4306