Part:BBa_K3182004

CHAP(K)

Staphylococcus phage endolysin, designed to target Staphylococcus aureus. This part was designed to be assembled with BBa_K3182010.

Bacteriophage endolysins digest the peptidoglycan wall of bacteria. The LysK is an endolysin targeting gram + bacteria. It has two catalytical domains known as CHAP (cysteine-and histidine depentent amidohydrolase/peptidase) and a central amidase-2 domain together with a cell binding domain. The CHAP domain which is the truncated part expressed in this year’s LiU iGEM (more specifically CHAP C1-C162) team still has lytic activity against staphylococcus. The C1 to C162 amino acids are required for full endopeptidase activity.

Figure 1. General mechanism of action when the antimicrobial agent is fused to BBa_K3182010 which contains the linker, thrombin site and cellulose binding domain. The cellulose binding domain enables the attachment of antimicrobial agents (such as antimicrobial peptide or enzyme) to the cellulose. This also inactivates the agents when they are expressed in its bacterial host. Later, when the bandage comes in contact with thrombin in the blood, the antimicrobial agents will be activated upon cleavage of its thrombin site.

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]