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Literature summary for 7.4.2.4 extracted from

  • Albiniak, A.M.; Baglieri, J.; Robinson, C.
    Targeting of lumenal proteins across the thylakoid membrane (2012), J. Exp. Bot., 63, 1689-1698.
    View publication on PubMed
Search for more literature for 7.4.2.4

Activating Compound

Activating Compound Comment Organism Structure
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
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

Inhibitors Comment Organism Structure
azide the translocation step across thylakoid membranes is inhibited by the SecA inhibitor azide Arabidopsis thaliana
azide the translocation step across thylakoid membranes is inhibited by the SecA inhibitor azide Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Zea mays 9507
-
chloroplast
-
 Arabidopsis thaliana 9507
-
thylakoid membrane integral membrane protein Zea mays 42651
-
thylakoid membrane integral membrane protein Arabidopsis thaliana 42651
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Zea mays
Mg2+ required Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Zea mays
-
 ADP + phosphate
-
 ?
ATP + H2O Arabidopsis thaliana
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-
Zea mays
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Zea mays
-
leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Zea mays ADP + phosphate
-
 ?
ATP + H2O
-
 Arabidopsis thaliana ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
SecA
-
 Zea mays
SecA
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
malfunction cpSecA absence can lead to severe defects in chloroplast sub-organelle structure and function Arabidopsis thaliana
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
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
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
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