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BimA
(Burkholderia intracellular motility A) |
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Belongs to the Oca/type Vc family of TAAs with a β barrel sequence and linker region with 48% similarity to the Y.enterocolitica YadA C-terminal (pfam domain 03895). The BimA passenger domain of B. pseudomallei, B. mallei and B. thailandensis differ markedly in primary sequence resulting in differences in the number of WH2 domains, sequence of proline-rich motifs and the presence of a central and acidic (CA) domain, indicating that they may initiate actin assembly by distinct mechanisms. ... |
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| ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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| RickA |
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Spotted fever group Rickettsia differ from other pathogens in possessing two actin-polymerizing proteins: RickA, an activator of the host Arp2/3 complex, and Sca2, a mimic of host formins. RickA generating short, curved actin tails early during infection and Sca2 generating long, straight actin tails later in infection. Considered a likely substrate of the rvh T4SS because of the lack of N-terminal Sec secretion signal and transmembrane spanning regions. ... |
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Sca2
(Surface cell antigen 2) |
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Similar to Listeria and Shigella, Rickettsia forms actin comet tails to propel its movement. However, the actin tails of Rickettsia consist of long and unbranched actin filaments, whereas those of Listeria and Shigella contain shorter and densely branched filaments. ... |
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IcsA (VirG)
(Ics for intercellular spread) |
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Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ... |
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BimA
(Burkholderia intracellular motility A) |
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Belongs to the Oca/type Vc family of TAAs with a β barrel sequence and linker region with 48% similarity to the Y.enterocolitica YadA C-terminal (pfam domain 03895). The BimA passenger domain of B. pseudomallei, B. mallei and B. thailandensis differ markedly in primary sequence resulting in differences in the number of WH2 domains, sequence of proline-rich motifs and the presence of a central and acidic (CA) domain, indicating that they may initiate actin assembly by distinct mechanisms. ... |
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BimA
(Burkholderia intracellular motility A) |
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Belongs to the Oca/type Vc family of TAAs with a β barrel sequence and linker region with 48% similarity to the Y.enterocolitica YadA C-terminal (pfam domain 03895). The BimA passenger domain of B. pseudomallei, B. mallei and B. thailandensis differ markedly in primary sequence resulting in differences in the number of WH2 domains, sequence of proline-rich motifs and the presence of a central and acidic (CA) domain, indicating that they may initiate actin assembly by distinct mechanisms. ... |
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BimA
(Burkholderia intracellular motility A) |
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Belongs to the Oca/type Vc family of TAAs with a β barrel sequence and linker region with 48% similarity to the Y.enterocolitica YadA C-terminal (pfam domain 03895). The BimA passenger domain of B. pseudomallei, B. mallei and B. thailandensis differ markedly in primary sequence resulting in differences in the number of WH2 domains, sequence of proline-rich motifs and the presence of a central and acidic (CA) domain, indicating that they may initiate actin assembly by distinct mechanisms. ... |
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BimA
(Burkholderia intracellular motility A) |
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Belongs to the Oca/type Vc family of TAAs with a β barrel sequence and linker region with 48% similarity to the Y.enterocolitica YadA C-terminal (pfam domain 03895). The BimA passenger domain of B. pseudomallei, B. mallei and B. thailandensis differ markedly in primary sequence resulting in differences in the number of WH2 domains, sequence of proline-rich motifs and the presence of a central and acidic (CA) domain, indicating that they may initiate actin assembly by distinct mechanisms. ... |
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BimA
(Burkholderia intracellular motility A) |
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Belongs to the Oca/type Vc family of TAAs with a β barrel sequence and linker region with 48% similarity to the Y.enterocolitica YadA C-terminal (pfam domain 03895). The BimA passenger domain of B. pseudomallei, B. mallei and B. thailandensis differ markedly in primary sequence resulting in differences in the number of WH2 domains, sequence of proline-rich motifs and the presence of a central and acidic (CA) domain, indicating that they may initiate actin assembly by distinct mechanisms. ... |
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