Literature summary for 3.4.21.89 extracted from

Fine, A.; Irihimovitch, V.; Dahan, I.; Konrad, Z.; Eichler, J.
Cloning, expression, and purification of functional Sec11a and Sec11b, type I signal peptidases of the archaeon Haloferax volcanii (2006), J. Bacteriol., 188, 1911-1919.

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Cloned(Commentary)

Cloned (Comment)	Organism
for purification purposes, tagged versions of the protein products of type I signal peptidase Sec11a and SEc11b are expressed in transformed Haloferax volcanii, with Sec11a or Sec11b being fused to a cellulose-binding domain capable of interaction with cellulose in hypersaline surroundings	Haloferax volcanii

Organism

Organism	UniProt	Comment	Textmining
Haloferax volcanii	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
for purification purposes, tagged versions of the protein products of type I signal peptidase Sec11a and SEc11b are expressed in transformed Haloferax volcanii, with Sec11a or Sec11b being fused to a cellulose-binding domain capable of interaction with cellulose in hypersaline surroundings	Haloferax volcanii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Clostridium thermocellum cellulose-binding domain containing a signal peptide + H2O	signal peptidase Sec11a and Sec11b cleave differentially	Haloferax volcanii	signal peptide + Clostridium thermocellum cellulose-binding domain	-	?

Synonyms

Synonyms	Comment	Organism
type I signal peptidase Sec11a	-	Haloferax volcanii
type I signal peptidase Sec11b	-	Haloferax volcanii

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Release 2023.1 (January 2023)