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Literature summary extracted from
- Targeting of lumenal proteins across the thylakoid membrane (2012), J. Exp. Bot., 63, 1689-1698.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.4.2.4 | additional information | 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 | Zea mays | |
| 7.4.2.4 | additional information | 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 | Arabidopsis thaliana |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.4.2.4 | azide | the translocation step across thylakoid membranes is inhibited by the SecA inhibitor azide | Arabidopsis thaliana |  |
| 7.4.2.4 | azide | the translocation step across thylakoid membranes is inhibited by the SecA inhibitor azide | Zea mays | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.4.2.4 | chloroplast | - |
Zea mays | 9507 | - |
| 7.4.2.4 | chloroplast | - |
Arabidopsis thaliana | 9507 | - |
| 7.4.2.4 | thylakoid membrane | integral membrane protein | Zea mays | 42651 | - |
| 7.4.2.4 | thylakoid membrane | integral membrane protein | Arabidopsis thaliana | 42651 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.4.2.4 | Mg2+ | required | Zea mays | |
| 7.4.2.4 | Mg2+ | required | Arabidopsis thaliana | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.4.2.4 | ATP + H2O | Zea mays | - |
ADP + phosphate | - |
? | |
| 7.4.2.4 | ATP + H2O | Arabidopsis thaliana | - |
ADP + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.4.2.4 | Arabidopsis thaliana | - |
- |
- |
| 7.4.2.4 | Zea mays | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 7.4.2.4 | leaf | - |
Zea mays | - |
| 7.4.2.4 | leaf | - |
Arabidopsis thaliana | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.4.2.4 | ATP + H2O | - |
Zea mays | ADP + phosphate | - |
? | |
| 7.4.2.4 | ATP + H2O | - |
Arabidopsis thaliana | ADP + phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.4.2.4 | SecA | - |
Zea mays |
| 7.4.2.4 | SecA | - |
Arabidopsis thaliana |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 7.4.2.4 | malfunction | cpSecA absence can lead to severe defects in chloroplast sub-organelle structure and function | Arabidopsis thaliana |
| 7.4.2.4 | metabolism | 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 | Zea mays |
| 7.4.2.4 | metabolism | 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 | Arabidopsis thaliana |
| 7.4.2.4 | 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 | Arabidopsis thaliana |
| 7.4.2.4 | 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 | Zea mays |
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