Protein Family Models

This domain is found at the N-terminus of the pre-pilin peptidases (Pfam:PF01478). Members of this entry have been characterised as bifunctional ([2]), and this domain may contain the N-methylation activity (EC:2.1.1.-). It consists of an intracellular region between a pair of transmembrane. This region contains an invariant proline and four almost fully conserved cysteines which bind Zn, as described for PilD from Pseudomonas aeruginosa [3]. The cysteines have been shown to be essential to the overall function of the enzyme [1,3]. [1]. 8340405. Identification of active-site cysteines in the conserved domain of PilD, the bifunctional type IV pilin leader peptidase/N-methyltransferase of Pseudomonas aeruginosa. Strom MS, Bergman P, Lory S;. J Biol Chem 1993;268:15788-15794. [2]. 8057924. Posttranslational processing of type IV prepilin and homologs by PilD of Pseudomonas aeruginosa. Strom MS, Nunn DN, Lory S;. Methods Enzymol 1994;235:527-540. [3]. 23255525. Cell-free production of integral membrane aspartic acid proteases reveals zinc-dependent methyltransferase activity of the Pseudomonas aeruginosa prepilin peptidase PilD. Aly KA, Beebe ET, Chan CH, Goren MA, Sepulveda C, Makino S, Fox BG, Forest KT;. Microbiologyopen. 2013;2:94-104. (from Pfam)

Date:

2024-10-16

Peptidase A24, or the prepilin peptidase as it is also known, processes the N-terminus of the prepilins [1]. The processing is essential for the correct formation of the pseudopili of type IV bacterial protein secretion. The enzyme is found across eubacteria and archaea [2]. [1]. 10625704. The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases. LaPointe CF, Taylor RK;. J Biol Chem 2000;275:1502-1510. [2]. 12813086. Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity. Albers SV, Szabo Z, Driessen AJ;. J Bacteriol 2003;185:3918-3925. (from Pfam)

Date:

2024-10-16

prepilin peptidase, A24 family peptidase, processes type 4 pilin precursor proteins (prepilins) to their mature forms by removal of leader peptides

Date:

2024-08-13