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Literature summary for 3.4.25.2 extracted from

  • Lien, H.Y.; Shy, R.S.; Peng, S.S.; Wu, Y.L.; Weng, Y.T.; Chen, H.H.; Su, P.C.; Ng, W.F.; Chen, Y.C.; Chang, P.Y.; Wu, W.F.
    Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system (2009), J. Bacteriol., 191, 4218-4231.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.25.2

Cloned(Commentary)

Cloned (Comment) Organism
genes clpY, co-expression of ClpQ and ClpY mutants in AC3112 cells. Co-expression of ClpY with HA-tagged SulA and mutant SulA M89I, RcsA, RpoH, and TraJ molecules in the yeast two-hybrid system, expression of recombinant ClpYQ mutants Escherichia coli

Protein Variants

Protein Variants Comment Organism
A188S clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview Escherichia coli
E193L/E194L clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview Escherichia coli
E61C clpQ mutant Escherichia coli
I186N clpY mutant, the mutant does not interact with SulA compared to the wild-type ClpY Escherichia coli
L199Q clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview. SulA accumulates in the bacterial cells that express ClpY Escherichia coli
M187I clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview Escherichia coli
additional information construction of truncation mutants lacking the substrate binding residues 137-209 of ClpY Escherichia coli
N141L/N142L the ClpY loop 1 mutant is defective in complete degradation of SulA Escherichia coli
N205K clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview Escherichia coli
Q148L/Q149L/Q150L the ClpY loop 1 mutant shows altered substrate recognition and binding, but shows normal activity similar to that of the wild-type ClpY Escherichia coli
Q198L/Q200L clpY mutant, the mutant shows altered interaction with SulA substrates, wild-type and mutant, and altered induction by arabinose or glutamate compared to the wild-type, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli in vivo, ClpYQ targets SulA, RcsA, RpoH, and TraJ molecules, identification of the molecular determinants required for the binding of its natural protein substrates by yeast two-hybrid analysis. Domain I of ClpY contains the residues, amino acids 137-150 of loop 1 and 175-209 of loop 2, double loops in domain I of ClpY, that are responsible for recognition of its natural substrates, while domain C is necessary to engage ClpQ, overview ?
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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.
additional information in vivo, ClpYQ targets SulA, RcsA, RpoH, and TraJ molecules, identification of the molecular determinants required for the binding of its natural protein substrates by yeast two-hybrid analysis. Domain I of ClpY contains the residues, amino acids 137-150 of loop 1 and 175-209 of loop 2, double loops in domain I of ClpY, that are responsible for recognition of its natural substrates, while domain C is necessary to engage ClpQ, overview Escherichia coli ?
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additional information ClpYQ is a two-component ATP-dependent protease in which ClpQ is the peptidase subunit and ClpY is the ATPase and the substrate-binding subunit. The ATP-dependent proteolysis is mediated by substrate recognition in the ClpYQ complex Escherichia coli ?
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Subunits

Subunits Comment Organism
More ClpYQ is a two-component ATP-dependent protease in which ClpQ is the peptidase subunit and ClpY is the ATPase and the substrate-binding subunit. ClpY has three domains, N, I, and C, and these domains are discrete and exhibit different binding preferences Escherichia coli

Synonyms

Synonyms Comment Organism
ClpYQ
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 Escherichia coli
ClpYQ protease
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 Escherichia coli
HslUV
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 Escherichia coli
HslUV protease
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 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli