v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | The Streptococcus pneumoniae psaA gene encodes a protein with significant similarity to previously-reported Streptococcal proteins, SsaB (80% similarity) and FimA (92.3% similarity), from Streptococcus sanguis and Streptococcus parasanguis [ ]. These homologues are associated with bacterial adhesion, and PsaA may play a similar role [].The SsaB protein has a putative hydrophobic 19-amino-acid signal sequence yielding a 32,620-Mr secreted protein [ ]. SsaB is hydrophilic and appears not to have a hydrophobic membrane anchor in its C-terminal region. A high degree of similarity exists between S. sanguis ssaB and type 1 fimbrial genes []. Comparison of the gene products reveals close similarity of the two proteins. It is thought that ssaB adhesion may play a role in oral colonisation by binding either to a receptor on saliva or to a receptor on Actinomyces.This sub-family is described by from conserved regions spanning the full alignment length, focusing on those sections that characterise the adhesin Bprecursors but distinguish them from the rest of the adhesin family. |
| Short Name | AdhesinB |