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Ata
(Acinetobacter trimeric autotransporter) |
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Important for adhesion to host extracellular matrices (collagen and laminin) and basal membrane components. ... |
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| BmaA |
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Monomeric autotransporter that shares significant sequence similarities with BmaC. The bmaA and bmaC loci from Brucella melitensis are pseudogenes. ... |
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| BmaB/OmaA |
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Monomeric autotransporter that shares significant sequence similarities with BmaC. Contributes to adhesion of B. suis to host cells as well as to extracellular matrix components such as fibronectin. ... |
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| BmaC |
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A large 340 kDa-protein with a long N-terminal cleavable 72 amino acid signal peptide and several adhesion-related motifs within the passenger domain, an extended pectin lyase virulence factor domain, and several passenger-associated-transport-repeats (PATR). ... |
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| BtaE |
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Both the BmaC and BtaE adhesins are consistently associated with the new cell pole, suggesting that, in Brucella, the new pole is functionally differentiated for adhesion. ... |
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| BtaF |
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Trimeric autotransporter involved in the adhesion to various ECM components (i.e. fibronectin, hyaluronic acid, fetuin, type I collagen) and to human cervical and alveolar epithelial cells. ... |
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Pmps
(Polymorphic membrane proteins) |
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The largest chlamydial protein family, with 9 members (subdivided into six subtypes) in C. trachomatis and 21 in C. pneumoniae, and are characterized by the presence of multiple copies of GGA(I,L,V) and FxxN motifs. Very heterogeneous not only in their number, but also in sequence. ... |
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| EspC |
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A large (110kDa) secreted protein of EPEC that does not require the TTSS for export. A member of the SPATE (serine protease autotransporters of the Enterobacteriaceae) family. espC gene located within a pathogenicity island at 60 min on the chromosome of E. coli, may play a role as an accessory virulence factor in some EPEC strains. ... |
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| EspP |
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Encoded within the pO157 plasmid. Serine protease. Cleaves coagulation factor V. ... |
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| EtpA |
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Interacts with highly conserved regions of flagellin exposed at the tips of flagella, exploiting these long (<10~15 mm) appendages to tether EtpA adhesins that anchor bacteria on initial engagement of host cells. ... |
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