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Abstract
The serine protease autotransporters of the Enterobacteriaceae (SPATEs) represent a group of large-sized, multi-domain exoproteins found only in pathogenic enteric bacteria. These proteins contain a highly conserved channel-forming C-terminal domain, which functions together with YaeT/Omp85 to facilitate secretion of the passenger domain to the cell surface. The C-terminal domain also mediates autoproteolytic cleavage, which releases the passenger from the bacterial cell. The passenger folds into a characteristic parallel beta-helical stalk-like structure with an N-terminal globular domain that performs serine proteolytic activity. Here, we review and discuss recent findings that have led to a better understanding of these unique features in this virulence protein family, including their biogenesis, structural architecture, sequence variation, sub-grouping, evolution and biochemical function.
Original language | English |
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Pages (from-to) | 370-379 |
Number of pages | 10 |
Journal | Trends in Microbiology |
Volume | 16 |
Issue number | 8 |
DOIs | |
Publication status | Published - 1 Aug 2008 |
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Dive into the research topics of 'Common themes and variations in serine protease autotransporters'. Together they form a unique fingerprint.Projects
- 1 Finished
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Understanding Events at the Cell Surface During Autotransporter Biogenesis
Henderson, I. (Principal Investigator) & Overduin, M. (Co-Investigator)
10/09/07 → 9/04/11
Project: Research Councils