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permease-like cell division protein FtsX
This is the extracellular domain (ECD) found in FtsX enzyme, a homolog of the transmembrane PG-hydrolase regulator. The FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that activates the enzyme ileading to PG hydrolysis in Mycobacterium tuberculosis. Structural analysis of FtsX ECD reveals fold containing two lobes connected by a flexible hinge. Mutations in the hydrophobic cleft between the lobes showed reduction in RipC binding in vitro and inhibition of FtsX function in Mycobacterium smegmatis [1]. [1]. 24843173. Mycobacterium tuberculosis FtsX extracellular domain activates. the peptidoglycan hydrolase, RipC.. Mavrici D, Marakalala MJ, Holton JM, Prigozhin DM, Gee CL, Zhang. YJ, Rubin EJ, Alber T;. Proc Natl Acad Sci U S A. 2014;111:8037-8042. (from Pfam)
FtsX-like permease family protein
This is a family of predicted permeases and hypothetical transmembrane proteins. Swiss:P57382 has been shown to transport lipids targeted to the outer membrane across the inner membrane. Both Swiss:P57382 and Swiss:O54500 have been shown to require ATP. This region contains three transmembrane helices. (from Pfam)
FtsX, a permease-like protein, forms a subcomplex with FtsE, an ABC transporter-like ATPase, as part of the divisome that carries out key steps of septum formation and cell separation in cell division. Rather than acting as a transporter, FtsEX transmits a mechanical signal from cytosol to periplasm to activate lytic enzymes there.
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