Information on EC 3.6.3.52 - chloroplast protein-transporting ATPase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.3.52
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RECOMMENDED NAME
GeneOntology No.
chloroplast protein-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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transmembrane transport
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (chloroplast protein-importing)
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process).
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gamma-subunit of enzyme
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Manually annotated by BRENDA team
gamma-subunit of enzyme
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
Hsp93/ClpC is a member of the Hsp100 family of chaperones, which itself belongs to the broader AAA+ (ATPases associated with various cellular activities) superfamily. Hsp100 proteins contain one or two AAA+ domains, and typically assemble into hexameric rings with a central pore through which substrate proteins can be threaded. Hsp100 proteins mediate ATP-dependent unfolding of proteins, in processes linked to protein degradation, protein disassembly, or protein trafficking across membranes; Hsp93/ClpC is a member of the Hsp100 family of chaperones, which itself belongs to the broader AAA+ (ATPases associated with various cellular activities) superfamily. Hsp100 proteins contain one or two AAA+ domains, and typically assemble into hexameric rings with a central pore through which substrate proteins can be threaded. Hsp100 proteins mediate ATP-dependent unfolding of proteins, in processes linked to protein degradation, protein disassembly, or protein trafficking across membranes
malfunction
metabolism
physiological function
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
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
azide
GTP
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inhibition of binding of transit peptide to chloroplast
Na3VO4
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reactive oxygen species
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reactive oxygen species dramatically decrease ATP synthesis in situ and affect the coupling factor CF1 portion in vitro. A conserved cluster of three methionines and a cysteine on the chloroplast gamma subunit are oxidized by reactive oxygen species. These residues are exclusive catalytic targets for hydrogen peroxide and singlet oxygen, although additional unknown amino acid targets might be involved in the latter reaction. The cluster is tightly integrated in catalytic turnover since mutants vary in MgATPase rates, stimulation by sulfite and chloroplast-specific gamma subunit redox-modulation
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
stromal protein factors
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additional information
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
associated to the membrane channel of the inner envelope membrane, at the stromal side; associated to the membrane channel of the inner envelope membrane, at the stromal side
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32500
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x * 47500 AtpA and AtpB, x * 32500 AtpC, SDS-PAGE
34000
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x * 34000, Toc34, + x * 75000, Toc75 + x * 159000, Toc159, Toc159 is originally identified as an 86000 Da polypeptide, designated Toc86, but it is shown that Toc86 is a proteolytic fragment of the native 159000 protein, the Toc components associate with three inner-membrane proteins, Tic110, Tic22 and Tic20, in a Toc-Tic supercomplex to form functional import sites
47500
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x * 47500 AtpA and AtpB, x * 32500 AtpC, SDS-PAGE
75000
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x * 34000, Toc34, + x * 75000, Toc75 + x * 159000, Toc159, Toc159 is originally identified as an 86000 Da polypeptide, designated Toc86, but it is shown that Toc86 is a proteolytic fragment of the native 159000 protein, the Toc components associate with three inner-membrane proteins, Tic110, Tic22 and Tic20, in a Toc-Tic supercomplex to form functional import sites
110000
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2 * 110000, SDS-PAGE
117000
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x * 117000, calculation from nucleotide sequence
159000
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x * 34000, Toc34, + x * 75000, Toc75 + x * 159000, Toc159, Toc159 is originally identified as an 86000 Da polypeptide, designated Toc86, but it is shown that Toc86 is a proteolytic fragment of the native 159000 protein, the Toc components associate with three inner-membrane proteins, Tic110, Tic22 and Tic20, in a Toc-Tic supercomplex to form functional import sites
200000
dimeric Hsp93-V/ClpC1 isoform; dimeric Hsp93-V/ClpC1 isoform
230000
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around, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
recombinant Hsp93-III/ClpC2 isozyme in solution is in dimeric form, upon addition of ATP, the hexamer state is observed. TIC-associated Hsp93 may act as a hexamer; recombinant Hsp93-III/ClpC2 isozyme in solution is in dimeric form, upon addition of ATP, the hexamer state is observed. TIC-associated Hsp93 may act as a hexamer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of Toc34, a regulatory component of the protein translocation machinerie at the outer envelope membrane of chloroplast
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expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expressed in green organs in a light-inducible way
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agy1
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a loss-of-function mutant of cpSecA, an albino or glassy yellow mutant, identified when screening a T-DNA insertion mutant collection. The mutant can grow normally on dim light with an exogenous carbon supply, but is subject to photo-oxidative stress in the light. Chloroplast biogenesis is clearly comprised in the mutant, and the transcription of both nucleus- and chloroplast-encoded photosynthetic proteins is repressed, whereas the transcription of mitochondrion-encoded respiratory complexes is induced
C199A/C205A
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ratio of MgATPase activity in reduced/oxidized state is 0.79, compared to 1.7 in wild-type
C89A
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ratio of MgATPase activity in reduced/oxidized state is 1.39, compared to 1.7 in wild-type
M231L
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ratio of MgATPase activity in reduced/oxidized state is 1.0, compared to 1.7 in wild-type
M23L/M279L/M282L
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ratio of MgATPase activity in reduced/oxidized state is 0.99, compared to 1.7 in wild-type
M23L/M279L/M282L/C89A
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ratio of MgATPase activity in reduced/oxidized state is 1.08, compared to 1.7 in wild-type
M279L/M282L
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ratio of MgATPase activity in reduced/oxidized state is 0.96, compared to 1.7 in wild-type
additional information
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gene disruption mutants of homologs atHSP93-V, atHSP93-III, mutant plants are much smaller and paler than wild-type plants, mutant chloroplasts contain less thylakoid membrane but are still able to import a variety of precursor proteins at reduced rate