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PROSITE documentation PDOC00571

Serine proteases, V8 family, active sites





Description

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.
Note:

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

Last update:

November 1995 / Patterns and text revised.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

V8_HIS, PS00672; Serine proteases, V8 family, histidine active site  (PATTERN)

V8_SER, PS00673; Serine proteases, V8 family, serine active site  (PATTERN)


References

1AuthorsDancer S.J. Garratt R. Saldanha J. Jhoti H. Evans R.
TitleThe epidermolytic toxins are serine proteases.
SourceFEBS Lett. 268:129-132(1990).
PubMed ID2384148

2AuthorsBailey C.J. Smith T.P.
TitleThe reactive serine residue of epidermolytic toxin A.
SourceBiochem. J. 269:535-537(1990).
PubMed ID9065774

3AuthorsSvendsen I. Breddam K.
TitleIsolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis.
SourceEur. J. Biochem. 204:165-171(1992).
PubMed ID1346764

4AuthorsSloma A. Rudolph C.F. Rufo G.A. Jr. Sullivan B.J. Theriault K.A. Ally D. Pero J.
TitleGene encoding a novel extracellular metalloprotease in Bacillus subtilis.
SourceJ. Bacteriol. 172:1024-1029(1990).
PubMed ID2105291

5AuthorsRawlings N.D. Barrett A.J.
TitleFamilies of serine peptidases.
SourceMethods Enzymol. 244:19-61(1994).
PubMed ID7845208

E1Titlehttps://www.uniprot.org/docs/peptidas



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