Protein Family Models

This entry represents two copies of a fourteen residue repeat that makes up the head domain of bacterial haemagglutinins and invasins. (from Pfam)

Date:

2024-08-14

This short motif is found in invasins and haemagglutinins, normally associated with (Pfam:PF05658). (from Pfam)

Date:

2024-08-14

This region represents the C-terminal 120 amino acids of a family of surface-exposed bacterial proteins. YadA, an adhesin from Yersinia, was the first member of this family to be characterised. UspA2 from Moraxella was second. The Eib immunoglobulin-binding proteins from E. coli were third, followed by the DsrA proteins of Haemophilus ducreyi and others. These proteins are homologous at their C-terminal and have predicted signal sequences, but they diverge elsewhere. The C-terminal 9 amino acids, consisting of alternating hydrophobic amino acids ending in F or W, comprise a targeting motif for the outer membrane of the Gram negative cell envelope. This region is important for oligomerisation [1]. [1]. 11705900. Nonimmune binding of human immunoglobulin A (IgA) and IgG Fc by distinct sequence segments of the EibF cell surface protein of Escherichia coli. Sandt CH, Hill CW;. Infect Immun 2001;69:7293-7303. [2]. 11080146. Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. Hoiczyk E, Roggenkamp A, Reichenbecher M, Lupas A, Heesemann J;. EMBO J 2000;19:5989-5999. (from Pfam)

Date:

2024-10-16

YadA C-terminal domain-containing protein similar to Yersinia enterocolitica trimeric autotransporter YadA, an non-fimbrial adhesin; YadA family autotransporter adhesin is a trimeric autotransporter, similar to Haemophilus influenzae Hia that mediates bacterial adhesion to the host respiratory epithelium

Date:

2017-03-02