Literature summary for 7.4.2.5 extracted from

de Keyzer, J.; van der Sluis, E.O.; Spelbrink, R.E.; Nijstad, N.; de Kruijff, B.; Nouwen, N.; van der Does, C.; Driessen, A.J.
Covalently dimerized SecA is functional in protein translocation (2005), J. Biol. Chem., 280, 35255-35260.

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General Stability

General Stability	Organism
SecYEG binding stabilizes a cold sodium dodecylsulfate-resistant dimeric state of SecA	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Escherichia coli	ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli	Escherichia coli	ADP + phosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	covalently dimerized SecA is functional in protein translocation	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ATPase SecA	-	Escherichia coli

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Release 2023.1 (January 2023)