Detail of GM0012
Summary
The genetically modified enzybiotic, named CHAP166 , constructed by Truncation strategy, decrease the lytic activity.With CHAP166
Sequence Length: 166 AA.
Mass: 18903.2 Da.
Isoelectric Point: 10.12
Function: CHAP domain with ~ 1.4-fold reduction in specific activity (0.023 ± 0.001 ΔOD600nm min-1µM-1) observed when compared to full-length HydH5 activity.
Construction
GM0012, constructed by Truncation strategy. No schema construted on GM0012
Details:
GM0012[1-166]: derive from protein B7T0E8 sequence 1-166
B7T0E8, 634 AA., the Gp58 from Staphylococcus phage phiSauS-IPLA88
Source: Staphylococcus phage phiSauS-IPLA88
483-629: IPR013338, the Lysozyme domain, subfamily 2
Biological Process: 0044036, the cell wall macromolecule metabolic process
Molecular Function: 0004040, the amidase activity?
Molecular Function: 0016787, the hydrolase activity?
Linking to UniprotKB
Linging to InterPro
Domains and repeats
15-149: IPR007921, the CHAP domain483-629: IPR013338, the Lysozyme domain, subfamily 2
GO term prediction
Biological Process: 0009253, the peptidoglycan catabolic processBiological Process: 0044036, the cell wall macromolecule metabolic process
Molecular Function: 0004040, the amidase activity?
Molecular Function: 0016787, the hydrolase activity?
Linking to UniprotKB
Linging to InterPro
Annotation
1-166
1-166
: EAD, CHAP domain, derived from Staphylococcus aureus bacteriophage vB_SauS-phi-IPLA88 endolysin HydH5;Domain and repeats:
15-149
: IPR007921,CHAP domain; GO term prediction:
MGLPNPKDRKPTASEVVEWALYMAKNRRVIDVDRSYGGQCWDVPNYILERYWGFRTWGNANAMAQKSNYRGRDFKIYRNTASFTPKPGDWAVWANRNPGHVAIVVGPADKNAFVSVDQNWYTANWSGSPPYKIKHTYHDGPGGVTHFVRPPYHPDKTTPAPQPVPK
Production
1. Expressed by pET27a in E. coli BL21(DE3), Purified by NiNTA nickel column chromatography (Qiagen, Valencia, CA).Activity
1. lytic activity test on Staphylococcus aureus (live S. aureus Sa9 cells ) by the turbidity-reduction assaysshowed specific activity of 0.023 ± 0.001 ∆OD600nm min-1µM-1