{PDOC51691}
{PS51691; PEPTIDASE_S6}
{BEGIN}
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* Peptidase family S6 domain profile *
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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 beta-
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  beta strands rolled into a barrel-like
structure with  several  long beta 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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2013 / First entry.

[ 1] Fink D.L., Cope L.D., Hansen E.J., St Geme J.W. III
     "The Hemophilus influenzae Hap autotransporter is a chymotrypsin clan
     serine protease and undergoes autoproteolysis via an intermolecular
     mechanism."
     J. Biol. Chem. 276:39492-39500(2001).
     PubMed=11504735; DOI=10.1074/jbc.M106913200
[ 2] Otto B.R., Sijbrandi R., Luirink J., Oudega B., Heddle J.G.,
     Mizutani K., Park S.-Y., Tame J.R.H.
     "Crystal structure of hemoglobin protease, a heme binding
     autotransporter protein  from pathogenic Escherichia coli."
     J. Biol. Chem. 280:17339-17345(2005).
     PubMed=15728184; DOI=10.1074/jbc.M412885200
[ 3] Meng G., Spahich N., Kenjale R., Waksman G., St Geme J.W. III
     "Crystal structure of the Haemophilus influenzae Hap adhesin reveals
     an intercellular oligomerization mechanism for bacterial
     aggregation."
     EMBO J. 30:3864-3874(2011).
     PubMed=21841773; DOI=10.1038/emboj.2011.279
[E1] https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=S6

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