Domain annotation of trimeric autotransporter adhesins—daTAA

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Domain annotation of trimeric autotransporter adhesins—daTAA

MOTIVATION Trimeric autotransporter adhesins (TAAs), such as Yersinia YadA, Neisseria NadA, Moraxella UspAs, Haemophilus Hia and Bartonella BadA, are important pathogenicity factors of proteobacteria. Their high sequence diversity and distinct mosaic-like structure lead to difficulties in the annotation of their sequences. These stem from the large number of short repeats, the presence of compo...

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Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter.

Autotransporter proteins are defined by the ability to drive their own secretion across the bacterial outer membrane. The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adhesion to the respiratory epithelium. In this report, we present the crystal structure of the C-terminal end of Hia, corresponding to the entire Hia trans...

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Structure of a Burkholderia pseudomallei Trimeric Autotransporter Adhesin Head

BACKGROUND Pathogenic bacteria adhere to the host cell surface using a family of outer membrane proteins called Trimeric Autotransporter Adhesins (TAAs). Although TAAs are highly divergent in sequence and domain structure, they are all conceptually comprised of a C-terminal membrane anchoring domain and an N-terminal passenger domain. Passenger domains consist of a secretion sequence, a head re...

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Domain Organization of Long Autotransporter Signal Sequences

Bacterial autotransporters represent a diverse family of proteins that autonomously translocate across the inner membrane of Gram-negative bacteria via the Sec complex and across the outer bacterial membrane. They often possess exceptionally long N-terminal signal sequences. We analyzed 90 long signal sequences of bacterial autotransporters and members of the two-partner secretion pathway in si...

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Molecular characterization of the EhaG and UpaG trimeric autotransporter proteins from pathogenic Escherichia coli.

Trimeric autotransporter proteins (TAAs) are important virulence factors of many Gram-negative bacterial pathogens. A common feature of most TAAs is the ability to mediate adherence to eukaryotic cells or extracellular matrix (ECM) proteins via a cell surface-exposed passenger domain. Here we describe the characterization of EhaG, a TAA identified from enterohemorrhagic Escherichia coli (EHEC) ...

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ژورنال

عنوان ژورنال: Bioinformatics

سال: 2008

ISSN: 1460-2059,1367-4803

DOI: 10.1093/bioinformatics/btn118