Protein Domain : IPR001872

Type:  Family Name:  Peptidase A8, signal peptidase II
Description:  Aspartic endopeptidases of vertebrate, fungal and retroviral origin have been characterised []. More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin [] and archaean preflagellin have been described [, ].Structurally, aspartic endopeptidases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localised between the two lobes of the molecule. One lobe has probably evolved from the other through a gene duplication event in the distant past. In modern-day enzymes, although the three-dimensional structures are very similar, the amino acid sequences are more divergent, except for the catalytic site motif, which is very conserved. The presence and position of disulphide bridges are other conserved features of aspartic peptidases. All or most aspartate peptidases are endopeptidases. These enzymes have been assigned into clans (proteins which are evolutionary related), and further sub-divided into families, largely on the basis of their tertiary structure.This group of aspartic peptidases belong to the MEROPS peptidase family A8 (signal peptidase II family, clan AC). The catalytic residues have not been identified, but three conserved aspartates can be identified from sequence alignments. The type example is the Escherichia colilipoprotein signal peptidase or SPase II (). This enzyme recognises 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 membrane.Bacterial cell walls contain large amounts of murein lipoprotein, a small protein that is both N-terminally bound to lipid and attached to membrane peptidoglycan (murein) through the epsilon-amino group of its C-terminal lysine residue [].Secretion of this lipoprotein is facilitated by the action of the lipoprotein signal peptidases in this entry, located in the inner membrane [, ]. They enzyme are inhibited by globomycinand also by pepstatin, suggesting that they are aspartic peptidases []. Short Name:  Peptidase_A8
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0 Child Features

0 Contains

5 Cross Referencess

Identifier
PF01252
PR00781
PS00855
TIGR00077
MF_00161

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0004190 IPR001872
GO:0006508 IPR001872
GO:0016020 IPR001872

3 Ontology Annotations

GO Term Gene Name
GO:0004190 IPR001872
GO:0006508 IPR001872
GO:0016020 IPR001872

0 Parent Features

6 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Brdisv1pangenome1001119m.p PAC:33620258 Brachypodium distachyon Pangenome 1637  
Brdisv1pangenome1007881m.p PAC:33622946 Brachypodium distachyon Pangenome 930  
Brdisv1pangenome1009117m.p PAC:33655990 Brachypodium distachyon Pangenome 1610  
Brdisv1BdTR11A1009828m.p PAC:35654558 Brachypodium distachyon BdTR11a 1637  
Brdisv1BdTR11A1043000m.p PAC:35690026 Brachypodium distachyon BdTR11a 930  
Brdisv1BdTR11A1040519m.p PAC:35692126 Brachypodium distachyon BdTR11a 1610  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID
            1455179
            14622420
            10625704
            16983194
            7674916
            6368552