1 Proteins
DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
---|---|---|---|---|
Araha.11756s0238.1.p | PAC:28856562 | Arabidopsis halleri |
406
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Type: | Family | Name: | HflK |
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. The HflK and HflC polypeptides are paralogous, and often encoded by tandem genes within bacterial genomes.This entry represents the HflK subunit of the HflKC heterodimer. | Short Name: | HflK |
DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
---|---|---|---|---|
Araha.11756s0238.1.p | PAC:28856562 | Arabidopsis halleri |
406
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