PROSITE documentation PDOC51691Peptidase family S6 domain profile
Autotransporters (ATs) represent a large superfamily of virulence factors produced by Gram-negative bacteria. ATs have evolved a unique export mechanism. Initially the protein is synthetized with an N-terminal leader peptide directing the protein to the periplasm via the signal recognition particle. Once accross the inner membrane, the C-terminal domain form a β-barrel structure (see <PDOC51208>) allowing the passenger domain to escape to the external medium, where it is released proteolytically from the cell. The 300-residue peptidase family S6 domain is found in a subfamily of autotransporter including:
- Neisseria gonorrhoeae IgA-specific serine endopeptidase autotransporter.
- Haemophilus influenzae immunoglobulin A1 protease autotransporter.
- Enteropathogenic Escherichia coli serine protease EspC.
- Enterohemorrhagic Escherichia coli serine protease EspP.
- Enteroaggregative Escherichia coli plasmid-encoded toxin (Pet).
- Uropathogenic Escherichia coli serine protease Sat autotransporter.
- Pathogenic Escherichia coli hemoglobin-binding protease Hbp autotransporter.
- Avian pathogenic Escherichia coli temperature-sensitive hemagglutinin Tsh autotransporter.
- Avian pathogenic Escherichia coli Vat.
- Shigella flexneri serine protease Pic autotransporter.
- Shigella flexneri serine protease SepA autotransporter.
The peptidase family S6 domain mediates intermolecular autoproteolysis, resulting in release of the passenger domain from the bacterial surface. It has a globular shape including six β strands rolled into a barrel-like structure with several long β hairpins over its surface (see <PDB:1WXR>). The catalytic triad is composed of Ser, Asp, and His [1,2,3].
The peptidase family S6 is a member of the SA (chymotrypsin) clan [1,E1].
The profile we developed covers the entire peptidase family S6 domain.
Last update:November 2013 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Fink D.L. Cope L.D. Hansen E.J. St Geme J.W. III |
| Title | The Hemophilus influenzae Hap autotransporter is a chymotrypsin clan serine protease and undergoes autoproteolysis via an intermolecular mechanism. | |
| Source | J. Biol. Chem. 276:39492-39500(2001). | |
| PubMed ID | 11504735 | |
| DOI | 10.1074/jbc.M106913200 |
| 2 | Authors | Otto B.R. Sijbrandi R. Luirink J. Oudega B. Heddle J.G. Mizutani K. Park S.-Y. Tame J.R.H. |
| Title | Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli. | |
| Source | J. Biol. Chem. 280:17339-17345(2005). | |
| PubMed ID | 15728184 | |
| DOI | 10.1074/jbc.M412885200 |
| 3 | Authors | Meng G. Spahich N. Kenjale R. Waksman G. St Geme J.W. III |
| Title | Crystal structure of the Haemophilus influenzae Hap adhesin reveals an intercellular oligomerization mechanism for bacterial aggregation. | |
| Source | EMBO J. 30:3864-3874(2011). | |
| PubMed ID | 21841773 | |
| DOI | 10.1038/emboj.2011.279 |
| E1 | Title | https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=S6 |
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