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Literature summary extracted from

  • Malet, H.; Canellas, F.; Sawa, J.; Yan, J.; Thalassinos, K.; Ehrmann, M.; Clausen, T.; Saibil, H.R.
    Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ (2012), Nat. Struct. Mol. Biol., 19, 152-157.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.107 structure determination and analysis of the 24meric enzyme with complexed substrate beta-casein, cryo-electron microscopy images and three-dimensional structures, overview Escherichia coli K-12

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.107 S187A a proteolytically inactive hexameric enzyme mutant Escherichia coli K-12

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.107 periplasm
-
 Escherichia coli K-12
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.107 44835
-
 12 * 44835, mass spectrometry Escherichia coli K-12
3.4.21.107 44835
-
 24 * 44835, mass spectrometry Escherichia coli K-12
3.4.21.107 44835
-
 6 * 44835, mass spectrometry Escherichia coli K-12
3.4.21.107 44840
-
 enzyme monomer, mass spectrometry Escherichia coli K-12
3.4.21.107 270100
-
 enzyme dodecamer, mass spectrometry Escherichia coli K-12
3.4.21.107 553100
-
 enzyme tetracosamer, mass spectrometry Escherichia coli K-12

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.107 additional information Escherichia coli K-12 the enzyme shows chaperone-like activity with substrate lysozyme, and protease activity. The PDZ domains are needed for DegQ chaperone activity. Up to six lysozyme substrates bind inside the DegQ dodecamer cage, binding of a well-ordered lysozyme to four DegQ protomers, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.107 Escherichia coli K-12 P39099
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.107 beta-casein + H2O
-
 Escherichia coli K-12 ?
-
 ?
3.4.21.107 additional information the enzyme shows chaperone-like activity with substrate lysozyme, and protease activity. The PDZ domains are needed for DegQ chaperone activity. Up to six lysozyme substrates bind inside the DegQ dodecamer cage, binding of a well-ordered lysozyme to four DegQ protomers, overview Escherichia coli K-12 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.107 dodecamer 12 * 44835, mass spectrometry Escherichia coli K-12
3.4.21.107 hexamer 6 * 44835, mass spectrometry Escherichia coli K-12
3.4.21.107 More DegQ changes its oligomeric state from hexamers to either 12 or 24mers depending on the concentration of unfolded substrate, DegQ forms 12mers in the absence of substrate at acidic pH, enzyme structure analysis of the 12 and 24mer states in complex with model substrates, overview. The polypeptides are probably cooperatively bound by PDZ1 and protease domains Escherichia coli K-12
3.4.21.107 tetracosamer 24 * 44835, mass spectrometry Escherichia coli K-12

Synonyms

EC Number Synonyms Comment Organism
3.4.21.107 DegQ
-
 Escherichia coli K-12

General Information

EC Number General Information Comment Organism
3.4.21.107 evolution the enzyme belongs to the HtrA protein family combines chaperone and protease activities and is essential for protein quality control in many organisms. HtrA proteins are composed of a chymotrypsin-like protease domain and one (DegS, HTRA1, HTRA2) or two PDZ domains (DegP, DegQ) Escherichia coli K-12
3.4.21.107 additional information enzyme structure analysis of the 12 and 24mer states in complex with model substrates, overview. DegQ PDZ domains are located adjacent to substrate density and their presence is required for chaperone activity Escherichia coli K-12