PASTA domain | |||||||||||
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Identifiers | |||||||||||
Symbol | PASTA | ||||||||||
Pfam | PF03793 | ||||||||||
InterPro | IPR005543 | ||||||||||
SMART | PASTA | ||||||||||
PROSITE | PDOC51178 | ||||||||||
SCOP2 | 1rp5 / SCOPe / SUPFAM | ||||||||||
CDD | cd06573 | ||||||||||
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The PASTA domain is a small protein domain that can bind to the beta-lactam ring portion of various β-lactam antibiotics.[1] The domain was initially discovered in 2002 by Yeats and colleagues as a region of sequence similarity found in penicillin binding proteins and PknB-like kinases found in some bacteria. The name is an acronym derived from PBP and Serine/Threonine kinase Associated domain.
The PASTA domain adopts a structure composed of an alpha-helix followed by three beta strands. Recent structural studies show that the extracellular region of PknB (protein kinase B) that is composed of four PASTA domains shows a linear arrangement of the domains.[2]
PASTA domains are found in a variety of bacterial species including gram-positive Bacillota and Actinomycetota.