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Information on EC 3.6.4.10 - non-chaperonin molecular chaperone ATPase

for references in articles please use BRENDA:EC3.6.4.10
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EC Tree
IUBMB Comments
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
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This record set is specific for:
UNIPROT: P22953
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
hsp90, heat shock protein, grp78, hsp60, groel, molecular chaperone, heat shock protein 70, hsc70, heat shock protein 90, hsp40, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular chaperone Hsc70 ATPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (polypeptide-polymerizing)
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Hsp70-1; isoform Hsp70-1
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
chloroplast stromal Hsp70s are believed to exist in a variety of plant species, including Arabidopsis, pea, poplar, rice, sorghum and moss
malfunction
the Arabidopsis Hsp70 knockout mutant cpshsc70-1 shows that stromal Hsp70 is important for the import of both photosynthetic and non-photosynthetic precursor proteins, especially at early developmental stages
metabolism
several chaperones and cochaperones mediate different stages of chloroplast import of preproteins, which are in a largely unfolded state. Cytosolic factors such as Hsp90, Hsp70 and 14-3-3 may assist preproteins to reach the TOC complex, i.e. translocon at the outer envelope membrane of chloroplasts complex, at the chloroplast surface, preventing their aggregation or degradation. Chaperones may also be involved in the intermembrane space transport. Preprotein translocation is completed at the trans side of the inner membrane by ATP-driven motor complexes. A stromal Hsp100-type chaperone, Hsp93, cooperates with Tic110 and Tic40 in one such motor complex, while stromal Hsp70 is proposed to act in a second, parallel complex. Upon arrival in the stroma, chaperones (e.g., Hsp70, Cpn60, cpSRP43) also contribute to the folding, assembly or onward intraorganellar guidance of the proteins. Chaperone involvement in the stroma during chloroplast protein import, modeling, detailed overview
physiological function
Hsp70 is involved in te chloroplast import of preproteins. Stromal Hsp70 might provide the driving force in chloroplast protein import. It may form a guidance complex together with 14-3-3 that delivers phosphorylated preproteins to the Toc34 receptor. Hsp70 is also proposed to deliver preproteins to the OEP61 protein
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HS701_ARATH
651
0
71358
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Flores-Perez, U.; Jarvis, P.
Molecular chaperone involvement in chloroplast protein import
Biochim. Biophys. Acta
1833
332-340
2013
Physcomitrium patens, Physcomitrium patens (D2XNF3), Physcomitrium patens (D2XNF4), Pisum sativum, Arabidopsis thaliana (P22953), Arabidopsis thaliana (P22954)
Manually annotated by BRENDA team