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Literature summary for 3.4.25.2 extracted from

  • Hsieh, F.C.; Chen, C.T.; Weng, Y.T.; Peng, S.S.; Chen, Y.C.; Huang, L.Y.; Hu, H.T.; Wu, Y.L.; Lin, N.C.; Wu, W.F.
    Stepwise activity of ClpY (HslU) mutants in the processive degradation of Escherichia coli ClpYQ (HslUV) protease substrates (2011), J. Bacteriol., 193, 5465-5476.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.25.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzyme sin Saccharomyces cerevisiae strain EGY48 containing plasmid BD-sulA or BD-sulA mutant M89I Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information enzyme inactivation by 7.5% SDS and 10% v/v 2-mercaptoethanol Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
SulA + H2O Escherichia coli the double loops, i.e amino acids 137 to 150 and 175 to 209, in domain I of ClpY are necessary for initial recognition/tethering of natural substrates such as SulA, a cell division inhibitor protein ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SulA + H2O the double loops, i.e amino acids 137 to 150 and 175 to 209, in domain I of ClpY are necessary for initial recognition/tethering of natural substrates such as SulA, a cell division inhibitor protein Escherichia coli ?
-
 ?
SulA + H2O a cell division inhibitor protein. Degradation of MBP-SulA by ClpY and ClpY mutants Y408A and T87I in the presence of ClpQ Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
ClpYQ
-
 Escherichia coli
HslUV
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on, an ATP-binding site in domain N, separate from its role in polypeptide, ClpY, oligomerization, is required for complex formation with ClpQ Escherichia coli
additional information no activity with ATP-gammaS analogue, thermodynamic analysis of ATP-gammaS-binding and ATPase activity of wild-type ClpY and its T87I mutant, overview. In the presence of MBP-SulA and ClpQ, the mutant has about one-fourth of the ATPase activity of wild-type ClpY, ClpY mutant T87I in its hexameric form is defective in ATPase activity Escherichia coli

General Information

General Information Comment Organism
additional information ClpYQ or HslUV is a two-component ATP-dependent protease composed of ClpY or HslU, an ATPase with unfolding activity, and ClpQ or HslV, a peptidase. In the ClpYQ proteolytic complex, the hexameric rings of ClpY (HslU) are responsible for protein recognition, unfolding, and translocation into the proteolytic inner chamber of the dodecameric ClpQ (HslV). The highly conserved sequence GYVG, residues 90 to 93, pore I site, along with the GESSG pore II site, residues 265 to 269, contribute to the central pore of ClpY in domain N. These two central loops of ClpY are in the center of its hexameric ring in which the energy of ATP hydrolysis allows substrate translocation and then degradation by ClpQ. The pore I site of ClpY has an effect on the adjoining structural region in protein substrates, and the pore I site is essential for the translocation of substrates. The pore II site also interfaces with nearby regions in the substrates but is not necessary for their translocation. An ATP-binding site in domain N, separate from its role in polypeptide, ClpY, oligomerization, is required for complex formation with ClpQ. Tyr408 in ClpY, like residue 385 in ClpX, is necessary for self-oligomerization, and this activity is likely important for in vivo protein-subunit stability Escherichia coli