Protein Family Models

Filamentous hemagglutinin (FHA), the major 230-kDa adhesin of the whooping cough agent Bordetella pertussis, is one of the most efficiently secreted proteins in Gram-negative bacteria. FHA is secreted by means of the two-partner secretion (TPS) pathway. A TPS system is composed of two separate proteins, with TpsA the secreted protein and TpsB its associated specific outer-membrane transporter. All TPS-secreted proteins contain a distinctive N-proximal module essential for secretion, the TPS domain. The TPS domain folds into a beta-helix. This domain is found in a wide variety of secreted proteins from bacterial pathogens. [1]. 15079085. The crystal structure of filamentous hemagglutinin secretion. domain and its implications for the two-partner secretion. pathway.. Clantin B, Hodak H, Willery E, Locht C, Jacob-Dubuisson F,. Villeret V;. Proc Natl Acad Sci U S A. 2004;101:6194-6199. (from Pfam)

Date:

2024-08-14

This HMM represents a conserved domain found near the N-terminus of a number of large, repetitive bacterial proteins, including many proteins of over 2500 amino acids. Members generally have a signal sequence, then an intervening region, then the region described by this HMM. Following this region, proteins typically have regions rich in repeats but may show no homology between the repeats of one member and the repeats of another. A number of the members of this family have been designated adhesins, filamentous haemagglutinins, heme/hemopexin-binding protein, etc.

Date:

2019-09-10