Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | SPASE_II |
Description
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 3.4.23.36), 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.
References
1.Signal peptidases in prokaryotes and eukaryotes--a new protease family. Dalbey RE, Von Heijne G. Trends Biochem. Sci. 17, 474-8, (1992). View articlePMID: 1455520
2.Nucleotide sequence of the Staphylococcus aureus signal peptidase II (lsp) gene. Zhao XJ, Wu HC. FEBS Lett. 299, 80-4, (1992). View articlePMID: 1544479