Part:BBa_K3187017

P22 Bacteriophage Coat Protein

LPETGG

name	LPETGG
basepairs	18
molecular weight	1478 Da
origin	synthetic
parts	basic part
properties	recognition sequence for sortase A

Usage and biology

Generally, the amino acid sequence LPXTG, where X can be every amino acid, is a recognition sequence. It is found in S. aureus and it is important for anchoring exoproteins in the peptidoglycan layer. Exoproteins are responsible for pathogenicity of the organism. LPXTG is recognized by sortase A, a transpeptidase which cleaves between the threonine (T) and the glycine (G). The threonine forms an amide bond with the pentaglycine sequence of the peptidoglycan layer. So, a covalent bond between protein and the outside of the peptidoglycan layer is produced. It has been shown that the sequence LPETG is well recognized by sortase A ^[1]. LPXTG is an easy opportunity to modify proteins, for example with peptides or other proteins that contains a polyG tag. We used a tag with four glycines BBa_K3187018. As a result, VLPs are easily modified too, because VLPs are made of proteins.
LPETGG can also be employed as a recognition sequence. The sequence shown below was derived from our main literature source ^[2] on which our project is based on.
LPETGG consists of 18 DNA base pairs and translates to a six amino acid sequence containing lysine, proline, glutamine acid, threonine and two glycines. The molecular weight of the peptide is 1478 Da.

References

↑ Silvie Hansenová Maňásková , Kamran Nazmi, Alex van Belkum, Floris J. Bikker, Willem J. B. van Wamel, Enno C. I. Veerman, Synthetic LPETG-Containing Peptide Incorporation in the Staphylococcus aureus Cell-Wall in a Sortase A- and Growth Phase-Dependent Manner, plos one, 19.02.2014 [1]
↑ Dustin Patterson,*,†Benjamin Schwarz,‡John Avera,‡Brian Western,†Matthew Hicks,†Paul Krugler,†Matthew Terra, †Masaki Uchida,‡Kimberly McCoy,‡and Trevor Douglas*,Sortase-Mediated Ligation as a Modular Approach for the Covalent Attachment of Proteins to the Exterior of the Bacteriophage P22Virus-like Particle, Bioconjugate Chemistry, 2017, 28, 2114−2124 [2]

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]

[1] Silvie Hansenová Maňásková , Kamran Nazmi, Alex van Belkum, Floris J. Bikker, Willem J. B. van Wamel, Enno C. I. Veerman, Synthetic LPETG-Containing Peptide Incorporation in the Staphylococcus aureus Cell-Wall in a Sortase A- and Growth Phase-Dependent Manner, plos one, 19.02.2014 [1]

[2] Dustin Patterson,*,†Benjamin Schwarz,‡John Avera,‡Brian Western,†Matthew Hicks,†Paul Krugler,†Matthew Terra, †Masaki Uchida,‡Kimberly McCoy,‡and Trevor Douglas*,Sortase-Mediated Ligation as a Modular Approach for the Covalent Attachment of Proteins to the Exterior of the Bacteriophage P22Virus-like Particle, Bioconjugate Chemistry, 2017, 28, 2114−2124 [2]

[1]

[2]