LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Family |
| Description | This family consists of a number of sequences which are highly similar to the Tir chaperone protein in Escherichia coli. In many Gram-negative bacteria, a key indicator of pathogenic potential is the possession of a specialised type III secretion system, which is utilised to deliver virulence effector proteins directly into the host cell cytosol. Many of the proteins secreted from such systems require small cytosolic chaperones to maintain the secreted substrates in a secretion-competent state. CesT serves a chaperone function for the enteropathogenic Escherichia coli (EPEC) translocated intimin receptor (Tir) protein, which confers upon EPEC the ability to alter host cell morphology following intimate bacterial attachment [ ]. This family also contains the chaperone protein sicP [ ] and several DspF and related sequences from several plant pathogenic bacteria. The "disease-specific"(dsp) region next to the hrp gene cluster of Erwinia amylovora is required for pathogenicity but not for elicitation of the hypersensitive reaction. DspF and AvrF are small (16kDa and 14kDa) and acidic with predicted amphipathic alpha helices in their C termini; they resemble chaperones for virulence factors secreted by type III secretion systems of animal pathogens [ ].This entry also includes Pseudomonas aeruginosa ExsC, which functions as a chaperone for ExsE. It is also part of the regulatory cascade that plays a role in the transcriptional regulation of the type III secretion system (T3SS) [ ]. The family also contains a number of proteins from eukaryotic parasites. |
| Short Name | Tir_chaperone |
