Part:BBa_K3805138

agrBD

This part is an important part of the agr system

agrD is a 138 bp sequence located in Staphylococcus aureus and has four different species, but all agrD sequences include an Asp-Glu motif followed immediately by an AIP sequence, and the amino-terminal portion of agrD has a conserved Ile-Gly motif. All precursor peptides of agrD have an amphipathic α-helix fragment, which is responsible for anchoring agrD to the cytoplasmic membrane. agrB is a 567bp sequence that transcribes a transmembrane protein with multiple active centres, the topology of which is not well understood. H77 and C84 are essential amino acids for the synthesis of active AIP. It has been suggested that AgrB is a cysteine protease involved in the first step of the AgrD process and produces an acylenzyme thioesterintermediate.

Although the information is not clear, it is certain that AgrD is a precursor peptide for AIPs and that AgrB functions as an enzyme in the post-processing of AgrD

AgrB plays an important role in the synthesis of AIPs. AgrB plays an important role in the synthesis of AIPs. At least four types of self-inducible peptides have been identified and their structures are shown in the diagram below.

Figure 1 Four AIP configurations

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

References

[1]Evolution of Multidrug Resistance during Staphylococcus aureus Infection Involves Mutation of the Essential Two Component Regulator WalKR[J] . Benjamin P. Howden,Christopher R. E. McEvoy,David L. Allen,Kyra Chua,Wei Gao,Paul F. Harrison,Jan Bell,Geoffrey Coombs,Vicki Bennett-Wood,Jessica L. Porter,Roy Robins-Browne,John K. Davies,Torsten Seemann,Timothy P. Stinear. PLOS Pathogens . 2011 (11)

[2]宋娟,楚雍烈.金黄色葡萄球菌基因调节系统研究进展[J].生命科学,2012,24(05):463-469.

[3]Biochemistry structure-activity analysis of synthetic autoinducing thiolactone peptidesfromStaphylococcus aureusresponsible for virulence. Patricia M,Guang Y J,Ronald B,et al. Proceedings of the National Academy of Sciences of the United States of America . 1999