IPR006129
Adhesin B
InterPro entry
Short name | AdhesinB |
family relationships |
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
[1]. These homologues are associated with bacterial adhesion, and PsaA may play a similar role
[1].
The SsaB protein has a putative hydrophobic 19-amino-acid signal sequence yielding a 32,620-Mr secreted protein
[2]. 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
[2]. 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 B precursors but distinguish them from the rest of the adhesin family.
References
1.Cloning and nucleotide sequence analysis of psaA, the Streptococcus pneumoniae gene encoding a 37-kilodalton protein homologous to previously reported Streptococcus sp. adhesins. Sampson JS, O'Connor SP, Stinson AR, Tharpe JA, Russell H. Infect. Immun. 62, 319-24, (1994). View articlePMID: 7505262
2.Nucleotide sequence of a gene coding for a saliva-binding protein (SsaB) from Streptococcus sanguis 12 and possible role of the protein in coaggregation with actinomyces. Ganeshkumar N, Hannam PM, Kolenbrander PE, McBride BC. Infect. Immun. 59, 1093-9, (1991). View articlePMID: 1671775
GO terms
Contributing Member Database Entry
- PRINTS:PR00691
Representative structure
3zk9: CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA D280N IN THE METAL-FREE, OPEN STATE