H
IPR038236

GlpG peptidase, N-terminal domain superfamily

InterPro entry
Short nameGlpG_N_sf
Overlapping entries
 

Description

This superfamily represents the N-terminal cytoplasmic domain of the rhomboid intra-membraneous serine protease GlpG, otherwise known as peptidase S54. It is not clear exactly what the function of this domain is in the protease, but its presence is critical for maintaining a catalytically competent state for the protein
[1]
.

The tertiary structure of the GlpG protein from Escherichia coli has been determined
[2]
. The GlpG protein has six transmembrane domains (other members of the family are predicted to have seven), with the N- and C-terminal ends anchored in the cytoplasm. One transmembrane domain is shorter than the rest, creating an internal, aqueous cavity just below the membrane surface and it is here were proteolysis occurs. There is also a membrane-embedded loop between the first and second transmembrane domains which is postulated to act as a gate controlling substrate access to the active site.

References

1.Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core. Sherratt AR, Blais DR, Ghasriani H, Pezacki JP, Goto NK. Biochemistry 51, 7794-803, (2012). View articlePMID: 22963263

2.The use of thioglycollate to demonstrate DNA AP (apurinic/apyrimidinic-site) lyase activities. Biological consequences of thiol addition to the 5' product of a beta-elimination reaction at an AP site in DNA. Bricteux-Gregoire S, Verly WG. Biochem. J. 273 ( Pt 3), 777-82, (1991). PMID: 1705116

Cross References

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