PROSITE documentation PDOC51178PASTA 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 <PDOC00100>) or transglycolase [1].
The PASTA domain is a small globular fold consisting of three β strands and an α helix, with a loop region of variable length between the first and second β strands (see <PDB:1QMF>) [1,2].
The profile we developed covers the entire PASTA domain.
Last update:December 2005 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Yeats C. Finn R.D. Bateman A. |
| Title | The PASTA domain: a beta-lactam-binding domain. | |
| Source | Trends. Biochem. Sci. 27:438-438(2002). | |
| PubMed ID | 12217513 |
| 2 | Authors | Gordon E. Mouz N. Duee E. Dideberg O. |
| Title | The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance. | |
| Source | J. Mol. Biol. 299:477-485(2000). | |
| PubMed ID | 10860753 | |
| DOI | 10.1006/jmbi.2000.3740 |
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