Pathways & interactions
Adhesion domain (IPR008966)
Short name: Adhesion_dom
The bacterial adhesion domain is found in adhesin proteins, which form part of the adhesive pilus found on the cell surface. Adhesin proteins are important for receptor binding to host cells during pathogenesis. For example, the Escherichia coli PapG adhesin at the tip of the P pilus is necessary for attachment to the human kidney receptor during pyelonephritis pathogenesis [PMID: 11440716]. The bacterial adhesion domain consists of a beta-sandwich formed of 9 strands in 2 sheets with a Greek-key topology and is a sub-class of the immunoglobin-like fold. Members of this structural superfamily include:
- Collagen-binding domain of adhesion [PMID: 9334749].
- Fibrinogen-binding domain, which is found in both fibrinogen-binding adhesion SdrG and in clumping factor A; these proteins contain a duplication of this domain, where each copy of this fold displays a variation in the core structure [PMID: 14567919].
- Pilus subunits, such as mannose-specific adhesion FimH (duplication of this domain), PapK pilus subunit (similar to C-terminal domain of FimH), PapE pilus subunit, and F1 capsule antigen Caf1 [PMID: 12010488].
- PapG adhesion receptor-binding domain [PMID: 11440716].
- F17c-type adhesions, such as fimbrail adhesion F17-AG lectin domain, and fimbrial lectin GafD [PMID: 12864853].
- Dr-family adhesion Afa-III [PMID: 15331605].
- SSF49401 (SSF49401)