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Gene Review:

hflC - FtsH protease regulator HflC

Escherichia coli CFT073

Kihara, A. et al., Noble, J.A. et al., Kihara, A. et al., Briere, L.A. et al., Schumann, W.

Schumann,

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Disease relevance of hflC

In Escherichia coli, FtsH forms a complex with a pair of periplasmically exposed membrane proteins, HflK and HflC [1].

High impact information on hflC

However, both its absence and overproduction stabilized cII in vivo and the proposed serine protease-like sequence motif in HflC was dispensable for the lysogenization control [2].
The C-terminal region of HflC contains a domain resembling the catalytic domain of ClpP, a bacterial ATP-dependent protease [3].
HflK and HflC are plasma membrane proteins of Escherichia coli, each having a large C-terminal domain exposed to the periplasmic space and an N-terminally located transmembrane segment, which should act as a signal anchor sequence for their biogenesis [4].
To test the importance of the small size of these positions, two residues in the HflC domain, Ala-262 in a f position and Gly-268 in an a position, were mutated to isoleucine [5].

References

FtsH--a single-chain charonin? Schumann, W. FEMS Microbiol. Rev. (1999) [Pubmed]
Host regulation of lysogenic decision in bacteriophage lambda: transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA). Kihara, A., Akiyama, Y., Ito, K. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain. Noble, J.A., Innis, M.A., Koonin, E.V., Rudd, K.E., Banuett, F., Herskowitz, I. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
Translocation, folding, and stability of the HflKC complex with signal anchor topogenic sequences. Kihara, A., Ito, K. J. Biol. Chem. (1998) [Pubmed]
The periplasmic domains of Escherichia coli HflKC oligomerize through right-handed coiled-coil interactions. Briere, L.A., Dunn, S.D. Biochemistry (2006) [Pubmed]

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