Your Input: | |||||
csgD | Putative 2-component transcriptional regulator for 2nd curli operon; Residues 1 to 216 of 216 are 99.07 pct identical to residues 1 to 216 of 216 from Escherichia coli K-12 Strain MG1655: B1040. (216 aa) | ||||
tir | Putative translocated intimin receptor protein; Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion. In strain EDL933, acts via the effector protein EspF(U), in a phosphotyrosine- and NCK- independent [...] (558 aa) | ||||
fliD | Flagellar biosynthesis; Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end (By similarity). (465 aa) | ||||
ycbB | Putative amidase; Residues 1 to 615 of 615 are 99.18 pct identical to residues 1 to 615 of 615 from Escherichia coli K-12 Strain MG1655: B0925. (615 aa) | ||||
htrA | Periplasmic serine protease Do; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essen [...] (474 aa) |