|SMART accession number:||SM00740|
|Interpro abstract (IPR005543):|
The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBP) and bacterial serine/threonine kinases. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. In PknB of Mycobacterium tuberculosis (P71584), all of the extracellular portion is predicted to be made up of four PASTA domains, which strongly suggests that it is a signal-binding sensor domain. The domain has also been found in proteins involved in cell wall biosynthesis, where it is implicated in localizing the biosynthesis complex to unlinked peptidoglycan.
PASTA is a small globular fold consisting of 3 beta-sheets and an alpha-helix, with a loop region of variable length between the first and second beta-strands. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain [(PUBMED:12217513)].
|GO function:||penicillin binding (GO:0008658)|
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- Evolution (species in which this domain is found)
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- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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