v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | The accumulation of abnormal membrane proteins is something which must be avoided in order to maintain cell viability. In Escherichia coli, the membrane-bound, ATP-dependent protease FtsH plays a central role in the degradation of these abnormal proteins [ ]. Known substrates of this protease include several lambda bacteriophage proteins, the heat-shock transcription factor sigma-32, and the unassembled form of the membrane protein SecY. While FtsH is active as a protease on its own, in vivo it forms a complex with a membrane-bound HflKC heterodimer. HflKC has a generally inhibitory effect on the protease activity of FtsH, though the mechanism of this inhibition is not known. HflK is a member of peptidase inhibitor family I87 []. The HflK and HflC polypeptides are paralogous, and often encoded by tandem genes within bacterial genomes.This entry represents the HflK subunit (MEROPS identifier I87.002) of the HflKC heterodimer. |
| Short Name | HflK |