Complete resonance assignments of the 'donor-strand complemented' AfaD: the afimbrial invasin from Diffusely Adherent E. coli.

The afa gene clusters encode afimbrial adhesins (AFAs) that are expressed by
uropathogenic and diarrhea-associated Escherichia coli strains. The
plasmid-borne afa-3 gene cluster is responsible for the biosynthesis of the
AFA-III adhesin that belongs to the Dr family of hemagglutinins. Reported in
this work is the nucleotide sequence of the 9.2-kb insert of the recombinant
plasmid pILL61, which contains the afa-3 gene cluster cloned from a
cystitis-associated E. coli strain (A30). The afa-3 gene cluster was shown to
contain six open reading frames, designated afaA to afaF. It was organized in
two divergent transcriptional units. Five of the six Afa products showed marked
homologies with proteins encoded by previously described adhesion systems that
allowed us to attribute to each of them a putative function in the biogenesis
of the AFA-III adhesin. AfaE was identified as the structural adhesin product,
whereas AfaB and AfaC were recognized as periplasmic chaperone and outer
membrane anchor proteins, respectively. The AfaA and AfaF products were shown
to be homologous to the PapI-PapB transcriptional regulatory proteins. No
function could be attributed to the AfaD product, the gene of which was
previously shown to be dispensable for the synthesis of a functional adhesin.
Upstream of the afa-3 gene cluster, a 1.2-kb region was found to be 96%
identical to the RepFIB sequence of one of the enterotoxigenic E. coli plasmids
(P307), suggesting a common ancestor plasmid. This region contains an
integrase-like gene (int). Sequence analysis revealed the presence of an IS1
element between the int gene and the afa-3 gene cluster. Two other IS1 elements
were detected and located in the vicinity of the afa-3 gene cluster by
hybridization experiments. The afa-3 gene cluster was therefore found to be
flanked by two IS1 elements in direct orientation and two in opposite
orientations. The afa-3 gene cluster, flanked by two directly oriented IS1
elements, was shown to translocate from a recombinant plasmid to the E. coli
chromosome. This translocation event occurred via IS1-specific recombination
mediated by a recA-independent mechanism.

Garcia MI, Labigne A, Le Bouguenec C.
Nucleotide sequence of the afimbrial-adhesin-encoding afa-3 gene cluster and
its translocation via flanking IS1 insertion sequences.
J Bacteriol. 1994 Dec;176(24):7601-13.

Nucleotide sequence of the afimbrial-adhesin-encoding afa-3 gene cluster and its translocation via flanking IS1 insertion sequences.

Structure Of Drad Invasin From Uropathogenic Escherichia Coli

The Fibrillar Tip Complex Of The AfaDR ADHESINS FROM Pathogen E. Coli Displays Synergistic Binding To 5 1 And V 3 Integrins

The Solution Structure Of The Invasive Tip Complex From Afa-Dr Fibrils

RecName: Full=Protein AfaD; Flags: Precursor [Escherichia coli]

Complete Resonance assignments of a donor-strand complemented AfaD: the
afimbrial invasin from Diffusely Adherent E. coli

Aria-implemented distance geometry, simulated annealing