Rhomboid protease

Rhomboid
Escherichia coli rhomboid protease GlpG in complex with a beta-lactam inhibitor (yellow) bound to the catalytic serine residue. From PDB: 3ZMH​.[1]
Identifiers
Symbol	Rhomboid
Pfam	PF01694
Pfam clan	CL0207
InterPro	IPR002610
MEROPS	S54
SCOP2	144092 / SCOPe / SUPFAM
OPM superfamily	165
OPM protein	2ic8
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

The rhomboid proteases are a family of enzymes that exist in almost all species. They are proteases: they cut the polypeptide chain of other proteins. This proteolytic cleavage is irreversible in cells, and an important type of cellular regulation. Although proteases are one of the earliest and best studied class of enzyme, rhomboids belong to a much more recently discovered type: the intramembrane proteases. What is unique about intramembrane proteases is that their active sites are buried in the lipid bilayer of cell membranes, and they cleave other transmembrane proteins within their transmembrane domains.^[2] About 30% of all proteins have transmembrane domains, and their regulated processing often has major biological consequences. Accordingly, rhomboids regulate many important cellular processes, and may be involved in a wide range of human diseases.