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Literature summary for 3.4.25.2 extracted from

  • Lee, Y.Y.; Chang, C.F.; Kuo, C.L.; Chen, M.C.; Yu, C.H.; Lin, P.I.; Wu, W.F.
    Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid system (2003), J. Bacteriol., 185, 2393-2401.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
RcsA + H2O positive regulator of capsule transcription, RcsA Escherichia coli ?
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RpoH + H2O RpoH is a heat shock sigma transcription factor Escherichia coli ?
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SulA + H2O cell division inhibitor SulA, the internal region of SulA is necessary for interactions with ClpY, the N-terminal amino acid residues of SulA are not necessary Escherichia coli additional information
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Subunits

Subunits Comment Organism
More ClpYQ is an ATP-dependent protease that consists of an ATPase large subunit, ClpY, and a peptidase small subunit, ClpQ. Six identical subunits of both ClpY and ClpQ self-assemble into an oligomeric ring, and two rings of each subunit, two ClpQ rings surrounded by single ClpY rings, form a dumbbell shape complex Escherichia coli