Common themes and variations in serine protease autotransporters.
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.
Yen
Yihfen T
YT
Department of Biological Sciences, California State Polytechnic University, Pomona, CA 91768, USA.
Kostakioti
Maria
M
Henderson
Ian R
IR
Stathopoulos
Christos
C
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics*; D017124:Conserved Sequence; D004755:Enterobacteriaceae / Q000201:enzymology*; D008958:Models, Molecular; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D012697:Serine Endopeptidases