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Information on EC 7.4.2.4 - chloroplast protein-transporting ATPase
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EC Tree
7.4.2.4 chloroplast protein-transporting ATPaseIUBMB Comments
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).
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Word Map
- 7.4.2.4
- oligomycin
- thylakoids
-
submitochondrial
-
translocon
- tic40
- dccd
- batten
-
photophosphorylation
-
hatefi
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blue-native
-
dccd-binding
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atpbe
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oligomycin-sensitive
The enzyme appears in viruses and cellular organisms
Synonyms
atp synthase complex, hsp93, cpseca, hsp93-v, rubisco small subunit transit peptide, sec-type system, atcpseca, sec translocase/integrase, rbcs tp, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cpSecA
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the ATPase subunit of the chloroplase Sec translocation machinery
EC 3.6.3.52
-
-
formerly
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hsp93
Sec-type system
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-
-
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Sec1
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the SEC1 system consists of two interacting membrane components, SCY1 and SECE1
SEC2
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the SEC1 system consists of two interacting membrane components, SCY2 and SECE2
SecA
SecA protein
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + chloroplast-protein[side 1] = ADP + phosphate + chloroplast-protein[side 2]
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. Involved in thetransport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process)
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-
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ATP + H2O + chloroplast-protein[side 1] = ADP + phosphate + chloroplast-protein[side 2]
interaction of transit peptide with translocation apparatus, identification of a chloroplast-binding intermediate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
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transmembrane transport
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-
-
-
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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).
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + chloroplast-protein[side 1]
ADP + phosphate + chloroplast-protein[side 2]
-
-
-
-
?
ATP + H2O + FTSH12 protein[side 1]
ADP + phosphate + FTSH12 protein[side 2]
-
-
-
-
?
ATP + H2O + heat shock protein 70[side 1]
ADP + phosphate + heat shock protein 70[side 2]
-
-
-
-
?
ATP + H2O + heat shock protein 90[side 1]
ADP + phosphate + heat shock protein 90[side 2]
-
-
-
-
?
ATP + H2O + heat shock protein 93[side 1]
ADP + phosphate + heat shock protein 93[side 2]
-
-
-
-
?
ATP + H2O + TIC110 protein[side 1]
ADP + phosphate + TIC110 protein[side 2]
-
-
-
-
?
ATP + H2O + TIC40 protein[side 1]
ADP + phosphate + TIC40 protein[side 2]
-
-
-
-
?
ATP + H2O
ADP + phosphate
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GTP requirement of the Toc complex is attributed to the GTPase component of the complex
-
?
ATP + H2O
ADP + phosphate
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involved in transport of proteins or preproteins into chloroplast stroma, the import process may be mediated by at least three discrete ATPases
-
?
ATP + H2O
ADP + phosphate
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the enzyme stimulates the in vitro import of the 33000 Da protein of the oxygen-evolving complex into thylakoids. SecA protein-dependent system is required for the intraorganellar protein transport
-
?
ATP + H2O
ADP + phosphate
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roles of DELTApH and ATP overlap and suggests that the DELTApH may be obligatory when the passenger protein is abnormally difficult to translocate
-
?
ATP + H2O
ADP + phosphate
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two distinct protein translocation machineries at the outer and inner chloroplast envelope membrane participate in the import of precursor proteins. The translocon at the outer envelope membrane of the chloroplast, Toc, mediates the initial binding of the cytosolic precursor proteins at the chloroplast surface and their subsequent ATP/GTP-dependent translocation across the outer membrane. Protein translocation across the inner membrane is mediated by the translocon at the inner envelope membrane of the chloroplast, Tic, and is driven by ATP hydrolysis in the stroma
-
?
ATP + H2O
ADP + phosphate
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two distinct protein translocation machineries at the outer and inner chloroplast envelope membrane participate in the import of precursor proteins. The translocon at the outer envelope membrane of the chloroplast, Toc, mediates the initial binding of the cytosolic precursor proteins at the chloroplast surface and their subsequent ATP/GTP-dependent translocation across the outer membrane. Protein translocation across the inner membrane is mediated by the translocon at the inner envelope membrane of the chloroplast, Tic, and is driven by ATP hydrolysis in the stroma
-
?
ATP + H2O
ADP + phosphate
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the enzyme facilitates transport of a subset of thylakoid lumenal proteins including the 33000 Da protein of the oxygen-evolving complex
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?
ATP + H2O
ADP + phosphate
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the ATPase does not function to generate a membrane potential for driving the import reaction
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?
ATP + H2O
ADP + phosphate
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the enzyme is required for the protein import from the cytoplasm into the chloroplast stroma
-
?
ATP + H2O
ADP + phosphate
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the Sec-type system is responsible for the translocation of a subset of proteins across the thylakoid membrane
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + chloroplast-protein[side 1]
ADP + phosphate + chloroplast-protein[side 2]
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
involved in transport of proteins or preproteins into chloroplast stroma, the import process may be mediated by at least three discrete ATPases
-
?
ATP + H2O
ADP + phosphate
-
the enzyme facilitates transport of a subset of thylakoid lumenal proteins including the 33000 Da protein of the oxygen-evolving complex
-
?
ATP + H2O
ADP + phosphate
-
the enzyme is required for the protein import from the cytoplasm into the chloroplast stroma
-
?
ATP + H2O
ADP + phosphate
-
the Sec-type system is responsible for the translocation of a subset of proteins across the thylakoid membrane
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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azide
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the translocation step across thylakoid membranes is inhibited by the SecA inhibitor azide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
stromal protein factors
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the transport of the 33000 Da protein of the oxygen evolving complexes and plastocyanin requires stromal factors and the thylakoid DELTApH
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stromal protein factors
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required for the transport of the 33000 Da protein of the oxygen evolving complexes
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additional information
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cpSecA ATPase activity is stimulated by cpSec-dependent thylakoid signal peptides, but not by Escherichia coli signal peptides, and stimulation of cpSecA ATPase activity exhibits specific lipid requirements
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additional information
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expression of nuclear-encoded SecA protein increases 3.7fold with increase in temperature from 30 to 40 and 50°C
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additional information
expression of nuclear-encoded SecA protein increases 3.7fold with increase in temperature from 30 to 40 and 50°C
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additional information
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expression of plastid-encoded SecA protein increases only slightly with increase in temperature from 30 to 40 and 50°C
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additional information
expression of plastid-encoded SecA protein increases only slightly with increase in temperature from 30 to 40 and 50°C
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anemia, Hypochromic
In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast protein import.
Carcinoma
Elastic-contractile model proteins: Physical chemistry, protein function and drug design and delivery.
Cardiomyopathies
Selective decrease of components of the creatine kinase system and ATP synthase complex in chronic Chagas disease cardiomyopathy.
Chagas Disease
Selective decrease of components of the creatine kinase system and ATP synthase complex in chronic Chagas disease cardiomyopathy.
Neuronal Ceroid-Lipofuscinoses
Abnormal degradative pathway of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid-lipofuscinosis (Batten disease).
Neuronal Ceroid-Lipofuscinoses
New insight into lysosomal protein storage disease: delayed catabolism of ATP synthase subunit c in Batten disease.
Neuronal Ceroid-Lipofuscinoses
Specific delay of degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis (Batten disease).
Obesity
Mitochondrial ATP synthase ?-subunit production rate and ATP synthase specific activity are reduced in skeletal muscle of humans with obesity.
Osteosarcoma
The Inhibitor Protein (IF1) of the F1F0-ATPase Modulates Human Osteosarcoma Cell Bioenergetics.
Retinoblastoma
Amplification of the gene encoding the alpha-subunit of the mitochondrial ATP synthase complex in a human retinoblastoma cell line.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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expressed in green organs in a light-inducible way
brenda
additional information
the expression of isozyme Hsp93-V is much higher than that of isozyme Hsp93-III
brenda
additional information
the expression of isozyme Hsp93-V is much higher than that of isozyme Hsp93-III
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
associated to the membrane channel of the inner envelope membrane, at the stromal side
brenda
in chloroplasts, Hsp93 can form part of the Clp protease complex (in a second role, additional to that in preprotein import), which recognizes and unfolds substrate proteins that are destined for degradation. Interaction of Hsp93 with the proteolytic ClpP core is ATP dependent
brenda
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Toc34, a regulatory component of the protein translocation machinery at the outer envelope membrane of chloroplast is tightly associated with the outer envelope membrane of chloroplast and exposed to the cytosol
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
malfunction
metabolism
physiological function
malfunction
Arabidopsis hsp93-V knockout plants are pale, with underdeveloped chloroplasts containing fewer thylakoid membranes and displaying reduced protein import efficiency. In contrast, hsp93-III knockout mutants are indistinguishable from wild-type. This can be explained by redundancy, as hsp93-III hsp93-V double mutants are embryo lethal and overexpression of Hsp93-III can complement hsp93-V, suggesting that the two isozyme proteins have overlapping functions and are able to partially substitute for each other in the single mutants
malfunction
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cpSecA absence can lead to severe defects in chloroplast sub-organelle structure and function
malfunction
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silencing of SCY2 and SCY1 results in chlorotic cotyledons. Null mutants of SCY2 in Arabidopsis (Arabidopsis thaliana) exhibit a severe embryo-lethal phenotype
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, EC 3.6.4.10, 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
metabolism
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two further pathways are used to translocate lumenal proteins across the thylakoid membrane from the stroma and, again, the two pathways differ dramatically from each other. One is a Sec-type pathway, in which ATP hydrolysis by SecA drives the transport of the substrate protein through the membrane in an unfolded conformation. The other is the twin-arginine translocation (Tat) pathway, where substrate proteins are transported in a folded state using a unique mechanism that harnesses the proton motive force across the thylakoid membrane. cpSecY and cpSecA work in concer in the Sec-type pathway. Targeting of proteins to the chloroplast thylakoid lumen, overview
metabolism
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two further pathways are used to translocate lumenal proteins across the thylakoid membrane from the stroma and, again, the two pathways differ dramatically from each other. One is a Sec-type pathway, in which ATP hydrolysis by SecA drives the transport of the substrate protein through the membrane in an unfolded conformation. The other is the twin-arginine translocation (Tat) pathway, where substrate proteins are transported in a folded state using a unique mechanism that harnesses the proton motive force across the thylakoid membrane. cpSecY and cpSecA work in concer in the Sec-type pathway. Targeting of proteins to the chloroplast thylakoid lumen, overview
metabolism
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the SEC2 translocase likely integrates a subset of inner envelope membrane proteins, such as FTSH12 and TIC40
physiological function
-
AtcpSecA plays an essential role in chloroplast biogenesis, structure and function, the absence of which triggers a retrograde signalling (chloroplast-to-mitochondrion) possibly leads to reprogramming of chloroplast and mitochondrion gene expression to alleviate photooxidative stress in order to survive with an insufficient energy supply
physiological function
the amount of nuclear-encoded SecA protein increases almost 4fold with increase in temperature, while the amount of plastid-encoded SecA protein increases only slightly. Data suggest an important role of nuclear-encoded SecA protein at high temperature
physiological function
the enzyme is involved in preprotein import into chloroplasts as a chaperone. Additionally, in chloroplasts, Hsp93 can form part of the Clp protease complex, which recognizes and unfolds substrate proteins that are destined for degradation. Interaction of Hsp93 with the proteolytic ClpP core is ATP dependent. The Tic110-Tic40 (Tic = translocon at the inner envelope membrane of chloroplasts) interaction triggers the release of the transit peptide from Tic110 and enables the association of the preprotein with Hsp93. Tic110 may dissociate from Tic40 when there is no transit peptide bound. The Tic40 Sti1 domain then stimulates ATP hydrolysis by Hsp93, which acts to pull the preprotein into the stroma using the released energy. Subsequently, Hsp93-ADP may dissociate from Tic40. TIC-associated hexameric Hsp93 may act by threading incoming preproteins through the axial channel of the complex. Hsp93/ClpC acts as a regulatory chaperone in the Clp protease, the Clp protease is essential for chloroplast development and plant viability
physiological function
-
the enzyme is required for the Sec-type pathway of chlorplastidic protein translocation, overview. The translocation step across thylakoid membranes is dependent on ATP. cpSecA is essential for photosynthetic development in Arabidopsis. The inability of the cpSec translocon to transport dihydrofolate reductase, in a methotrexate-stabilized folded conformation, demonstrates that the cpSec pathway in plants requires protein substrates to be in an unfolded state for transport
physiological function
-
the enzyme is required for the Sec-type pathway of chlorplastidic protein translocation, overview. The translocation step across thylakoid membranes is dependent on ATP. The inability of the cpSec translocon to transport dihydrofolate reductase, in a methotrexate-stabilized folded conformation, demonstrates that the cpSec pathway in plants requires protein substrates to be in an unfolded state for transport
physiological function
-
SCY2 plays an essential role in chloroplast biogenesis beyond embryo development
physiological function
-
the SEC1 system is particularly important for the biogenesis of soluble lumenal proteins or thylakoid membrane proteins with large lumenal domains. Proteins that are unfolded travel via the central channel of the SEC translocase
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
159000
-
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
34000
-
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
75000
-
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
?
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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
additional information
-
the pore-forming subunit of the translocon of the outer envelope of the chloroplast, Toc75 transverses the outer envelope with 16 amphiphilic beta sheets
additional information
-
analysis of protein-protein interactions using epitope-tagged transit peptide, identification of a chloroplast-binding intermediate
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
removal of 20 or 23 amino acid residues from the center of the transit peptide of ATPase gamma subunit reduces in vitro import to chloroplasts to an undetectable level but does not affect subunit accumulation in vivo
proteolytic modification
-
enzyme import into plastid is a two-step event, transit peptide-like domain of enzyme is functionally equivalent to the respective targeting signal of higher plants
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agy1
-
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
-
ratio of MgATPase activity in reduced/oxidized state is 0.79, compared to 1.7 in wild-type
C89A
-
ratio of MgATPase activity in reduced/oxidized state is 1.39, compared to 1.7 in wild-type
M231L
-
ratio of MgATPase activity in reduced/oxidized state is 1.0, compared to 1.7 in wild-type
M23L/M279L/M282L
-
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
-
ratio of MgATPase activity in reduced/oxidized state is 0.96, compared to 1.7 in wild-type
additional information
-
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
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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
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scott, S.V.; Theg, S.M.
A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: enegetics and mechanistic implications
J. Cell Biol.
132
63-75
1996
Pisum sativum
brenda
Nakai, M.; Goto, A.; Nohara, T.; Sugita, D.; Endo, T.
Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoid protein transport
J. Biol. Chem.
269
31338-31341
1994
Pisum sativum
brenda
Hirohashi, T.; Nakai, M.
Molecular cloning and characterization of maize Toc34, a regulatory component of the protein import machinery of chloroplast
Biochim. Biophys. Acta
1491
309-314
2000
Pisum sativum, Zea mays
brenda
Chen, K.; Chen, X.; Schnell, D.J.
Mechanism of protein import across the chloroplast envelope
Biochem. Soc. Trans.
28
485-491
2000
Pisum sativum
brenda
Nohara, T.; Nakai, M.; Goto, A.; Endo, T.
Isolation and characterization of the cDNA for pea chloroplast SecA evolutionary conservation of the bacterial type SecA-dependet protein transport within chloroplasts
FEBS Lett.
364
305-308
1995
Pisum sativum
brenda
Hulford, A.; Hazell, L.; Mould, R.M.; Robinson, C.
Two distinct mechanisms for the translocation of proteins across the thylakoid membrane, one requiring the presence of a stromal protein factor and nucleotide triphosphates
J. Biol. Chem.
269
3251-3256
1994
Pisum sativum
brenda
Pain, D.; Blobel, G.
Protein import into chloroplasts requires a chloroplast ATPase
Proc. Natl. Acad. Sci. USA
84
3288-3292
1987
Pisum sativum
brenda
Berghoefer, J.; Karnauchov, I.; Herrmann, R.G.; Kloesgen, R.B.
Isolation and characterization of a cDNA encoding the SecA protein from spinach chloroplasts. Evidence for azide resistance of Sec-dependent protein translocation across thylakoid membranes in spinach
J. Biol. Chem.
270
18341-18346
1995
Spinacia oleracea
brenda
Mant, A.; Schmidt, I.; Herrmann, R.G.; Robinson, C.; Kloesgen, R.B.
Sec-dependent thylakoid protein translocation. DELTApH requirement is dictated by passenger protein and ATP concentration
J. Biol. Chem.
270
23275-23281
1995
Pisum sativum
brenda
Sveshnikova, N.; Grimm, R.; Soll, J.; Schleiff, E.
Topology studies of the chloroplast protein import channel Toc75
Biol. Chem.
381
687-693
2000
Pisum sativum
brenda
Lang, M.; Apt, K.E.; Kroth, P.G.
Protein transport into "complex" diatom plastids utilizes two different targeting signals
J. Biol. Chem.
273
30973-30978
1998
Trieres chinensis
brenda
Subramanian, C.; Ivey, R.3rd.; Bruce, B.D.
Cytometric analysis of an epitope-tagged transit peptide bound to the chloroplast translocation apparatus
Plant J.
25
349-363
2001
Pisum sativum
brenda
Kindle, K.L.; Lawrence, S.D.
Transit peptide mutations that impair in vitro and in vivo chloroplast protein import do not affect accumulation of the gamma-subunit of chloroplast ATPase
Plant Physiol.
116
1179-1190
1998
Chlamydomonas reinhardtii
brenda
Constan, D.; Froehlich, J.E.; Rangarajan, S.; Keegstra, K.
A stromal hsp100 protein is required for normal chloroplast development and function in Arabidopsis
Plant Physiol.
136
3605-3615
2004
Arabidopsis thaliana
brenda
Kanervo, E.; Singh, M.; Suorsa, M.; Paakkarinen, V.; Aro, E.; Battchikova, N.; Aro, E.
Expression of protein complexes and individual proteins upon transition of etioplasts to chloroplasts in pea (Pisum sativum)
Plant Cell Physiol.
49
396-410
2008
Pisum sativum
brenda
Liu, D.; Gong, Q.; Ma, Y.; Li, P.; Li, J.; Yang, S.; Yuan, L.; Yu, Y.; Pan, D.; Xu, F.; Wang, N.N.
cpSecA, a thylakoid protein translocase subunit, is essential for photosynthetic development in Arabidopsis
J. Exp. Bot.
61
1655-1669
2010
Arabidopsis thaliana
brenda
Buchert, F.; Schober, Y.; Roempp, A.; Richter, M.L.; Forreiter, C.
Reactive oxygen species affect ATP hydrolysis by targeting a highly conserved amino acid cluster in the thylakoid ATP synthase gamma subunit
Biochim. Biophys. Acta
1817
2038-2048
2012
Spinacia oleracea
brenda
Koyama, Y.; Kaneko, Y.; Matsuoka, S.; Matsumoto, K.; Hara, H.; Ohta, N.
Expression and localization of two SecA homologs in the unicellular red alga Cyanidioschyzon merolae
Biosci. Biotechnol. Biochem.
76
417-422
2012
Cyanidioschyzon merolae, Cyanidioschyzon merolae (Q85G35)
brenda
Flores-Perez, U.; Jarvis, P.
Molecular chaperone involvement in chloroplast protein import
Biochim. Biophys. Acta
1833
332-340
2013
Arabidopsis thaliana (Q9FI56), Arabidopsis thaliana (Q9SXJ7)
brenda
Albiniak, A.M.; Baglieri, J.; Robinson, C.
Targeting of lumenal proteins across the thylakoid membrane
J. Exp. Bot.
63
1689-1698
2012
Arabidopsis thaliana, Zea mays
brenda
Fernandez, D.E.
Two paths diverged in the stroma targeting to dual SEC translocase systems in chloroplasts
Photosynth. Res.
138
277-287
2018
Arabidopsis thaliana
brenda
Li, Y.; Martin, J.R.; Aldama, G.A.; Fernandez, D.E.; Cline, K.
Identification of putative substrates of SEC2, a chloroplast inner envelope translocase
Plant Physiol.
173
2121-2137
2017
Arabidopsis thaliana
brenda
Lee, D.W.; Yoo, Y.J.; Razzak, M.A.; Hwang, I.
Prolines in transit peptides are crucial for efficient preprotein translocation into chloroplasts
Plant Physiol.
176
663-677
2018
Arabidopsis thaliana
brenda
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EXTERNAL LINKS (specific for EC-Number 7.4.2.4)
Transporter Classification Database (TCDB): 3.A.5.4.2
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Release 2023.1 (January 2023)
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