Protein Domain : Dr-adhesin superfamily IPR037028

Type	Homologous_superfamily
Description	Dr-adhesin bind the Dr blood group antigen component of decay-accelerating factor. These proteins contain both fimbriated and afimbriated adherence structures and mediate adherence of uropathogenic Escherichia coli to the urinary tract [ ]. They also confer the mannose-resistant hemagglutination phenotype, which can be inhibited by chloramphenicol. The N-terminal portion of the mature protein is thought to be responsible for chloramphenicol sensitivity [].Afa/Dr adhesins display an afimbrial/fimbrial morphology and are exported to the bacterial surface by the chaperone-usher pathway, a widespread system among gram-negative pathogens for the secretion of fimbrial proteins [ ]. AfaD protein caps the AfaE fibrils, where it can efficiently perform its role as an invasin [].The structure of the AfaD domain exhibits an Immunoglobulin-like topology where the two β-sheets pack against each other in an analogous fashion to AfaE and archetypal pilin domains. The AfaD role as an initiator of the fimbrial assembly and the cap of the fibrillar structure is defined by the absence of a free N-terminal extension [ ].
Short Name	Dr_adhesin_sf