{PDOC00571}
{PS00672; V8_HIS}
{PS00673; V8_SER}
{BEGIN}
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* Serine proteases, V8 family, active sites *
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A number of prokaryotic proteases  have  been  shown [1,2] to  be evolutionary
related; their catalytic activity is provided by a charge relay system similar
to that of the trypsin family  of  serine proteases but which probably evolved
by independent convergent evolution. The sequence around the residues involved
in  the catalytic  triad (aspartic acid, serine and histidine) are  completely
different from that of the analogous residues  in the trypsin serine proteases
and can be  used as signatures  specific  to  that category of proteases.  The
proteases which are known to belong to this family are listed below.

 - Staphylococcus aureus V8 proteinase, which preferentially  cleaves  peptide
   bonds on the carboxyl-terminal side of aspartate and glutamate and which is
   widely used in protein sequencing studies.
 - Bacillus licheniformis glutamate  specific  endopeptidase (GSE) [3],  which
   like V8 cleaves on the carboxyl-terminal  side of acidic residues, but with
   a strong preference for glutamate.
 - Bacillus subtilis extracellular "metalloprotease" (gene mpr) [4].
 - Staphylococcus aureus exfoliative  (or epidermolytic)  toxins  A (gene eta)
   and B (gene etb).  These toxins cause impetigous diseases commonly referred
   to as staphylococcal scalded  skin syndrome (SSSS) and  have been shown [1]
   to possess proteolytic activity.

-Consensus pattern: [ST]-G-[LIVMFYW](3)-[GN]-x(2)-T-[LIVM]-x-T-x(2)-H
                    [H is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: T-x(2)-[GC]-[NQ]-S-G-S-x-[LIVM]-[FY]
                    [The first S is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: These proteins belong to family S2B in the classification of peptidases
 [5,E1].

-Last update: November 1995 / Patterns and text revised.

[ 1] Dancer S.J., Garratt R., Saldanha J., Jhoti H., Evans R.
     "The epidermolytic toxins are serine proteases."
     FEBS Lett. 268:129-132(1990).
     PubMed=2384148
[ 2] Bailey C.J., Smith T.P.
     "The reactive serine residue of epidermolytic toxin A."
     Biochem. J. 269:535-537(1990).
     PubMed=9065774
[ 3] Svendsen I., Breddam K.
     "Isolation and amino acid sequence of a glutamic acid specific
     endopeptidase from Bacillus licheniformis."
     Eur. J. Biochem. 204:165-171(1992).
     PubMed=1346764
[ 4] Sloma A., Rudolph C.F., Rufo G.A. Jr., Sullivan B.J., Theriault K.A.,
     Ally D., Pero J.
     "Gene encoding a novel extracellular metalloprotease in Bacillus
     subtilis."
     J. Bacteriol. 172:1024-1029(1990).
     PubMed=2105291
[ 5] Rawlings N.D., Barrett A.J.
     "Families of serine peptidases."
     Methods Enzymol. 244:19-61(1994).
     PubMed=7845208
[E1] https://www.uniprot.org/docs/peptidas

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