Difference between revisions of "Part:BBa K257018"

Revision as of 16:40, 21 October 2009

AIDA-I autotransporter, linker + translocator domains

The cell envelope of gram-negative bacteria consists of two membranes, the cytoplasmic or inner membrane and the outer membrane. Transport of proteins across the inner membrane in most cases follows the general secretory pathway (GSP). Therefore, in gram-negative bacteria, proteins end up in the periplasm. To translocate proteins to the outer surface or into the supernatant, gram-negative bacteria have developed several distinct mechanisms. In contrast to the secretory systems that require a variety of specialized accessory proteins that, often in combination with the GSP, are responsible for the export of one or several passenger proteins into the supernatant, the autotransporter protein family members carry the export signal and machinery within a single polypeptide chain. The adhesin-involved-in-diffuse-adherence (AIDA) autotransporter has been identified as a virulence factor of the enteropathogenic Escherichia coli strain 2787 and predicted to be a member of the autotransporter protein family. AIDA-I is the adhesin involved in diffuse adherence of E.coli. It belongs to the monomeric autotransporter protein family of the type-V secretion pathway. AIDA-I is synthesized from the aidA gene as a 145 kDa pre-proprotein with three domains : first, an N-terminal sec-dependent signal sequence that allows transport across the inner membrane; second, a cenral domain of 100kDa, the mature AIDA-I, bearing the functional part of the protein; and finally, a C-terminal membrane-embedded domain of 45kDa, AIDAc, which is predicted to form a pore in the outer membrane and might serve as a translocation conduit for mature AIDA-I.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BamHI site found at 1118
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 __NOTOC__
 <partinfo>BBa_K257018 short</partinfo>
+The cell envelope of gram-negative bacteria consists of two membranes, the cytoplasmic or inner membrane and the outer membrane. Transport of proteins across the inner membrane in most cases follows the general secretory pathway (GSP). Therefore, in gram-negative bacteria, proteins end up in the periplasm. To translocate proteins to the outer surface or into the supernatant, gram-negative bacteria have developed several distinct mechanisms. In contrast to the secretory systems that require a variety of specialized accessory proteins that, often in combination with the GSP, are responsible for the export of one or several passenger proteins into the supernatant, the autotransporter protein family members carry the export signal and machinery within a single polypeptide chain. The adhesin-involved-in-diffuse-adherence (AIDA) autotransporter has been identified as a virulence factor of the enteropathogenic Escherichia coli strain 2787 and predicted to be a member of the autotransporter protein family.
 AIDA-I is the adhesin involved in diffuse adherence of E.coli. It belongs to the monomeric autotransporter protein family of the type-V secretion pathway. AIDA-I is synthesized from the aidA gene as a 145 kDa pre-proprotein with three domains : first, an N-terminal sec-dependent signal sequence that allows transport across the inner membrane; second, a cenral domain of 100kDa, the mature AIDA-I, bearing the functional part of the protein; and finally, a C-terminal membrane-embedded domain of 45kDa, AIDAc, which is predicted to form a pore in the outer membrane and might serve as a translocation conduit for mature AIDA-I.