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Information on EC 5.6.1.7 - chaperonin ATPase

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IUBMB Comments
Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. They are a subclass of molecular chaperones that are related to EC 3.6.4.8 (proteasome ATPase).
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Word Map
  • 5.6.1.7
  • heat-shock
  • rrna
  • mycobacterial
  • refolding
  • chlamydia
  • actin
  • humoral
  • misfolded
  • tubulins
  • helicobacter
  • bovis
  • encapsulation
  • pylori
  • trachomatis
  • avium
  • autoantibody
  • immunodominant
  • non-native
  • dna-dna
  • toll-like
  • ifn-gamma
  • rhodanese
  • pcr-restriction
  • leprae
  • autoantigens
  • tick-borne
  • endosymbiotic
  • polyphasic
  • co-chaperone
  • soda
  • tick
  • equatorial
  • multilocus
  • concatenate
  • rubisco
  • endosymbionts
  • thermotolerance
  • mycolic
  • atp-driven
  • cryo-electron
  • rickettsia
  • ixodes
  • aggregation-prone
  • tubal
  • candidatus
  • mg-atp
  • acid-fast
  • clarithromycin
  • proteostasis
  • medicine
  • haeiii
  • molecular biology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
a folded polypeptide
=
+
+
an unfolded polypeptide
Synonyms
alpha chaparonin, ApcpnA, archael group II chaperonin, archaeosome, bacterial chaperonin, bacteriophage-version of GroES, CCT, CCT1, CCT2, CCT3, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
show the reaction diagram