F
IPR006128

Adhesion lipoprotein PsaA-like

InterPro entry
Short nameLipoprotein_PsaA-like
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
[1]
. PsaA is part of the ATP-binding cassette (ABC) transport system PsaABC involved in manganese import
[3, 4]
. It binds manganese with high affinity and specificity and delivers it to the membrane permease for translocation into the cytoplasm
[4]
. PsaA also acts as an adhesin which is involved on adherence to extracellular matrix being an important factor in pathogenesis and infection
[3]
.

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 family includes adhesins and related periplasmic binding proteins.

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

3.Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases. Dintilhac A, Alloing G, Granadel C, Claverys JP. Mol. Microbiol. 25, 727-39, (1997). View articlePMID: 9379902

4.A molecular mechanism for bacterial susceptibility to zinc. McDevitt CA, Ogunniyi AD, Valkov E, Lawrence MC, Kobe B, McEwan AG, Paton JC. PLoS Pathog. 7, e1002357, (2011). View articlePMID: 22072971

GO terms

biological process

molecular function

  • None

cellular component

  • None
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