{PDOC51178} {PS51178; PASTA} {BEGIN} ************************ * PASTA domain profile * ************************ The PASTA domain (for penicillin-binding protein and serine/threonine kinase associated domain) is an extracellular module of ~70 residues that is found in the C-termini of eukaryotic-like serine/threonine kinases (PSTKs) and high molecular weight penicilin-binding proteins (PBPs). The PASTA domain is distributed mainly in the GRAM-positive bacteria, most notably among species of the genera Bacillus and Clostridia. It is not found in eukaryotes. The PASTA domain occurs both singly and in multiple copies, which suggests that it is a domain rather than a structural repeat. It is found in association with other domains, such as transpeptidase, protein kinase (see ) or transglycolase [1]. The PASTA domain is a small globular fold consisting of three beta strands and an alpha helix, with a loop region of variable length between the first and second beta strands (see ) [1,2]. The profile we developed covers the entire PASTA domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2005 / First entry. [ 1] Yeats C., Finn R.D., Bateman A. "The PASTA domain: a beta-lactam-binding domain." Trends. Biochem. Sci. 27:438-438(2002). PubMed=12217513 [ 2] Gordon E., Mouz N., Duee E., Dideberg O. "The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance." J. Mol. Biol. 299:477-485(2000). PubMed=10860753; DOI=10.1006/jmbi.2000.3740 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}