ATP-Dependent Zinc Metalloprotease Ftsh (ftsH) Escherichia Coli Recombinant Protein

HtpX collaborates with FtsH to eliminate abnormal membrane proteins: an hflX ftsH double mutant is temperature sensitive for growth. [More information is available at EcoGene: EG11506]. FtsH is a membrane-bound, ATP-dependent metalloprotease which has been shown to be involved in the degradation of some aberrant membrane and cytoplasmic proteins . [More information is available at EcoCyc: EG11506].

Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F0 ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, this probably requires ATP. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS).MiscellaneousThe ftsH gene was discovered independently through 3 different phenotypes and received 3 different names: ftsH, for filamentous temperature-sensitive; tolZ, for colicin tolerance, and hlfB, because mutants show a high frequency of lysogenization when infected with phage lambda.