Literature summary for 3.4.21.105 extracted from

Wang, Y.; Ha, Y.
Open-cap conformation of intramembrane protease GlpG (2007), Proc. Natl. Acad. Sci. USA, 104, 2098-2102.

Search for more literature for 3.4.21.105

Crystallization (Commentary)

Crystallization (Comment)	Organism
GlpG in a more open conformation, where the capping loop L5 has been lifted, exposing the previously buried and catalytically essential Ser201 to outside aqueous solution, X-ray diffraction structure determination and analysis at 2.5-2.6 A resolution	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	the internal and hydrophilic active site of the intramembrane protease is positioned in the lipid bilayer to facilitate peptide bond hydrolysis in the membrane	Escherichia coli	16020	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09391	gene glpG	-

Reaction

Reaction	Comment	Organism	Reaction ID
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains	catalytic mechanism, structure of the active site within the membrane, residues Ser201, His150, and Asn154 are important in catalysis, overview	Escherichia coli	a

Subunits

Subunits	Comment	Organism
More	GlpG structure and active site structure, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
GlpG	-	Escherichia coli
intramembrane protease	-	Escherichia coli
More	GlpG belongs to the intramembrane protease rhomboid family	Escherichia coli

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Release 2023.1 (January 2023)