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Literature summary for 3.6.4.10 extracted from

  • Sugimoto, S.; Yoshida, H.; Mizunoe, Y.; Tsuruno, K.; Nakayama, J.; Sonomoto, K.
    Structural and functional conversion of molecular chaperone ClpB from the gram-positive halophilic lactic acid bacterium Tetragenococcus halophilus mediated by ATP and stress (2006), J. Bacteriol., 188, 8070-8078.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.10

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Tetragenococcus halophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Tetragenococcus halophilus enzyme forms dimers and monomers to function as a holding chaperone under stress conditions, whereas it forms a hexamer ring to function as a chaperone in cooperation with KJE and ATP under poststress conditions ?
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 ?

Organism

Organism UniProt Comment Textmining
Tetragenococcus halophilus
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 isoform ClpB
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Purification (Commentary)

Purification (Comment) Organism
recombinant protein Tetragenococcus halophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme forms dimers and monomers to function as a holding chaperone under stress conditions, whereas it forms a hexamer ring to function as a chaperone in cooperation with KJE and ATP under poststress conditions Tetragenococcus halophilus ?
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 ?
additional information the hexameric, nonstress form of ClpB reactivates heat-aggregated proteins dependent on the DnaK system and ATP. The mixture of dimer and monomer, which is formed under stress conditions, protects substrate proteins from thermal inacivation and aggregation Tetragenococcus halophilus ?
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 ?

Subunits

Subunits Comment Organism
dimer and monomer, under stress conditions such as temperature above 45°C, or more than 1 M KCl, electron microscopy Tetragenococcus halophilus
hexamer in presence of ATP, under nonstress conditions, electron microscopy Tetragenococcus halophilus
monomer and dimer, under stress conditions such as temperature above 45°C, or more than 1 M KCl, electron microscopy Tetragenococcus halophilus