PROSITE documentation PDOC00669
Signal peptidases II signature


Signal peptidases (SPases) [1] (also known as leader peptidases) remove the signal peptides from secretory proteins. In prokaryotes three types of SPases are known: type I (gene lepB) which is responsible for the processing of the majority of exported pre-proteins; type II (gene lsp) which only process lipoproteins, and a third type involved in the processing of pili subunits.

SPase II (EC, also known as lipoprotein signal peptidase, recognizes a conserved sequence and cuts in front of a cysteine residue to which a glyceride-fatty acid lipid is attached. SPase II is an integral membrane protein that is anchored in the cytoplasmic membrane.

There are a number of conserved regions in the sequence of Spase II from various bacteria [2], we have selected one of these regions as a signature pattern.


These proteins belong to family A8 in the classification of peptidases [3,E1].

Expert(s) to contact by email:

von Heijne G.

Last update:

April 2006 / Pattern revised.


Technical section

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

SPASE_II, PS00855; Signal peptidases II signature  (PATTERN)


1AuthorsDalbey R.E. Von Heijne G.
TitleSignal peptidases in prokaryotes and eukaryotes--a new protease family.
SourceTrends Biochem. Sci. 17:474-478(1992).
PubMed ID1455520

2AuthorsZhao X.J. Wu H.C.
TitleNucleotide sequence of the Staphylococcus aureus signal peptidase II (lsp) gene.
SourceFEBS Lett. 299:80-84(1992).
PubMed ID1544479

3AuthorsRawlings N.D. Barrett A.J.
TitleEvolutionary families of metallopeptidases.
SourceMethods Enzymol. 248:183-228(1995).
PubMed ID7674922


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