Detail of GM0124
Summary
The genetically modified enzybiotic, named B30-182 , constructed by Truncation strategy, keep the lytic activity.With B30-182
Sequence Length: 182 AA.
Mass: 19989 Da.
Isoelectric Point: 4.52
Function: keep the lytic activity
Construction
GM0124, constructed by Truncation strategy. No schema construted on GM0124
Details:
GM0124[1-182]: derive from protein Q5MY96 sequence 1-182
Q5MY96, 443 AA., the Lysin PlyGBS from Streptococcus phage NCTC11261
Source: Streptococcus phage NCTC11261
152 - 339: IPR017853, the Glycoside hydrolase, superfamily
390 - 437: IPR003646, the SH3-like domain, bacterial-type
Biological Process: 0009253, the peptidoglycan catabolic process
Biological Process: 0016998, the cell wall macromolecule catabolic process
Molecular Function: 0003796, the lysozyme activity
Linking to UniprotKB
Linging to InterPro
Domains and repeats
1 - 131: IPR007921, the CHAP domain152 - 339: IPR017853, the Glycoside hydrolase, superfamily
390 - 437: IPR003646, the SH3-like domain, bacterial-type
GO term prediction
Biological Process: 0005975, the carbohydrate metabolic processBiological Process: 0009253, the peptidoglycan catabolic process
Biological Process: 0016998, the cell wall macromolecule catabolic process
Molecular Function: 0003796, the lysozyme activity
Linking to UniprotKB
Linging to InterPro
Annotation
1-182
1-182
: EAD, CHAP domain, derived from S. agalactiae bacteriophage endolysin B30;: EAD, Amidase domain, derived from S. agalactiae bacteriophage endolysin B31;
Domain and repeats:
1-182
: IPR017853,Glycoside hydrolase, superfamily; 1-182
: IPR003646,SH3-like domain, bacterial-type; 1-182
: IPR007921,CHAP domain; GO term prediction:
MATYQEYKSRSNGNAYDIDGSFGAQCWDGYADYCKYLGLPYANCTNTGYARDIWEQRHENGILNYFDEVEVMQAGDVAIFMVVDGVTPYSHVAIFDSDAGGGYGWFLGQNQGGANGAYNIVKIPYSATYPTAFRPKVFKNAVTVTGNIGLNKGDYFIDVSAYQQADLTTTCQQAGTTKTIIK