Peptidase_U4 |
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PFAM accession number: | PF03419 |
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Interpro abstract (IPR005081): | Sporulation in bacteria such as Bacillus subtilis involves the formation of a polar septum, which divides the sporangium into a mother cell and a forespore. The sigma E factor, which is encoded within the spoIIG operon, is a cell-specific regulatory protein that directs gene transcription in the mother cell. Sigma E is synthesised as an inactive proprotein pro-sigma E, which is converted to the mature factor by the processing enzyme SpoIIGA, releasing an N-terminal peptide [ (PUBMED:11849534) ]. The SpoIIGA peptidase (MEROPS peptidase family A36) is assumed to be an aspartic peptidase because of the presence of an Asp-Thr/Ser-Gly motif in which the Asp is an active site residue. The peptidase is active as a homodimer [ (PUBMED:18378688) ]. SpoIIGA has five transmembrane helices at the N-terminal half of the molecule; the proteolytic activity is in the C-terminal half [ (PUBMED:3125985) ]. Its tertiary structure is not known. |
GO process: | asexual sporulation (GO:0030436), proteolysis (GO:0006508) |
GO function: | aspartic-type endopeptidase activity (GO:0004190) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_U4