Function and Biology

Structure of E.coli rhomboid protease GlpG in complex with monobactam L62

Source organism: Escherichia coli
Biochemical function: serine-type endopeptidase activity
Biological process: proteolysis
Cellular component: integral component of membrane

EC 3.4.21.105: Rhomboid protease

Reaction catalysed:
Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Comments:
  • These endopeptidases are multi-spanning membrane proteins.
  • Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains.
  • Important for embryo development in Drosophila melanogaster.
  • Rhomboid is a key regulator of EGF receptor signaling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway.
  • Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.
  • Belongs to peptidase family S54.
Systematic name:
-

GO terms

Biochemical function:
Biological process:
Cellular component:

Sequence family

InterPro InterPro annotations
IPR035952
Domain description: Rhomboid-like superfamily
Occurring in:
  1. Rhomboid protease GlpG
IPR022764
Domain description: Peptidase S54, rhomboid domain
Occurring in:
  1. Rhomboid protease GlpG
IPR023662
Domain description: Rhomboid protease GlpG
Occurring in:
  1. Rhomboid protease GlpG
IPR002610
Domain description: Peptidase S54, rhomboid
Occurring in:
  1. Rhomboid protease GlpG

Structure domain

CATH CATH domain
1.20.1540.10
Class: Mainly Alpha
Architecture: Up-down Bundle
Topology: Rhomboid-like fold
Homology: Rhomboid-like domains
Occurring in:
  1. Rhomboid protease GlpG
1 copy of CATH domain 1.20.1540.10 (Rhomboid-like fold) in Rhomboid protease GlpG in PDB 3zmh.