| Primary Identifier | IPR019758 | Type | Conserved_site |
| Short Name | Pept_S26A_signal_pept_1_CS |
| description | Signal peptidases (SPases) [](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 processlipoproteins, and a third type involved in the processing of pili subunits.SPase I (EC 3.4.21.89) is an integral membrane protein that is anchored in the cytoplasmic membrane by one (in Bacillus subtilis) or two (in Escherichia coli) N-terminal transmembrane domains with the main part of the protein protuding in the periplasmic space. Two residues have been shown [, ]to be essential for the catalytic activity of SPase I: a serine and an lysine.SPase I is evolutionary related to the yeast mitochondrial inner membraneprotease subunit 1 and 2 (genes IMP1 and IMP2) which catalyse the removal ofsignal peptides required for the targeting of proteins from the mitochondrialmatrix, across the inner membrane, into the inter-membrane space [].In eukaryotes the removal of signal peptides is effected by an oligomericenzymatic complex composed of at least five subunits: the signal peptidasecomplex (SPC). The SPC is located in the endoplasmic reticulum membrane. Twocomponents of mammalian SPC, the 18 Kd (SPC18) and the 21 Kd (SPC21) subunitsas well as the yeast SEC11 subunit have been shown []to share regions ofsequence similarity with prokaryotic SPases I and yeast IMP1/IMP2.This entry represents a conserved region of unknown biological significance which is located in the C-terminal section of S26 peptidases (SPase I and IMP1/2). |
