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:

2024-08-14

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