Literature summary for 7.4.2.5 extracted from

Deitermann, S.; Sprie, G.S.; Koch, H.G.
A dual function for SecA in the assembly of single spanning membrane proteins in Escherichia coli (2005), J. Biol. Chem., 280, 39077-39085.

Search for more literature for 7.4.2.5

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Escherichia coli	ATP hydrolysis by SecA is required only if periplasmic loops larger than 30 amino acids have to be translocated. The signal recognition particle-dependent and SecA-dependent multiple spanning membrane protein YidC becomes SecA-independent if the large periplasmic loop connecting transmembrane domains 1 and 2 is reduced to less than 30 amino acids. The SecA dependence of a bacterial membrane protein is not solely determined by the length of the periplasmic loop but also by the presence of a down-stream TM domain	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	ATP hydrolysis by SecA is required only if periplasmic loops larger than 30 amino acids have to be translocated. The signal recognition particle-dependent and SecA-dependent multiple spanning membrane protein YidC becomes SecA-independent if the large periplasmic loop connecting transmembrane domains 1 and 2 is reduced to less than 30 amino acids. The SecA dependence of a bacterial membrane protein is not solely determined by the length of the periplasmic loop but also by the presence of a down-stream TM domain	Escherichia coli	ADP + phosphate	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)