Literature summary for 3.5.1.108 extracted from

Fuehrer, F.; Mueller, A.; Baumann, H.; Langklotz, S.; Kutscher, B.; Narberhaus, F.
Sequence and length recognition of the C-terminal turnover element of LpxC, a soluble substrate of the membrane-bound FtsH protease (2007), J. Mol. Biol., 372, 485-496.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

General Information

General Information	Comment	Organism
metabolism	the membrane-anchored FtsH protease is essential in Escherichia coli as it adjusts the cellular amount of LpxC, the key enzyme in lipopolysaccharide biosynthesis. Both accumulation and depletion of LpxC are toxic to Escherichia coli. By continuous proteolysis of LpxC, FtsH maintains a low concentration of LpxC and, hence, the proper equilibrium between lipopolysaccharide and phospholipids. The C terminus of LpxC is required for turnover. Detailed mutational analysis revealed six non-polar residues in the C terminus of LpxC that are critical for degradation	Escherichia coli

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Release 2023.1 (January 2023)