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9CAUD:Q8LTE6
Contents
| Species (Taxon ID) | Bacillus phage Gamma. (347962) | |
| Gene Name(s) | PlyG (ECO:0000313 with EMBL:ABB55421.1) | |
| Protein Name(s) | N-acetylmuramoyl-L-alanine amidase (ECO:0000313 with EMBL:AAM97149.1) | |
| External Links | ||
| UniProt | Q8LTE6 | |
| EMBL | AF536823 DQ222853 DQ222855 DQ221100 | |
| RefSeq | YP_338200.1 | |
| PDB | 2L47 2L48 | |
| PDBsum | 2L47 2L48 | |
| SMR | Q8LTE6 | |
| GeneID | 3703711 | |
| EvolutionaryTrace | Q8LTE6 | |
| GO | GO:0046872 GO:0008745 GO:0009253 | |
| Gene3D | 3.40.80.10 | |
| InterPro | IPR021976 IPR002502 | |
| Pfam | PF12123 PF01510 | |
| SMART | SM00644 | |
| SUPFAM | SSF55846 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0044659 |
viral release from host cell by cytolysis |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Figure 3 shows Plyg induced lysis of Bacillus anthracis cells and cell membranes |
complete | ||||
|
Contributes to |
GO:0009253 |
peptidoglycan catabolic process |
ECO:0000247 |
sequence alignment evidence used in manual assertion |
|
P |
Figure 1a in the literature shows a schematic representation of PlyG and PlyL, and the umbers of amino acid residues involved in catalysis are respectively, 233 and 234, indicating a high sequence similarity and low E-value, allowing assumption of function similarity to the endolysin PlyL. In addition, figure 2a, shows a sequence alignment of PlyG and PlyL and PlyG has a high degree of sequence similarity to PlyL. There are only 10 amino acid residue differences within the N-terminal regions of PlyG and PlyL, while 30 amino acid residues are different within their C-terminal regions. Therefore, it seems likely that the N-terminal region of PlyG also has similar characteristics. |
complete | ||
|
involved_in |
GO:0044659 |
cytolysis by virus of host cell |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
| GO:0051672 |
catabolism by organism of cell wall peptidoglycan in other organism |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Figure 2d. in the literature compares Lytic activities of wild-type PlyG and its C-terminal deletion mutant. Catalytic activity was examined by colony-forming assay, and the control, PlyGB, was set to 100%. As shown in the figure, deletion of the C-terminal region completely abolished the lytic ability of PlyG, with the colony forming units of the C-terminal deletion mutant at a very high percentage, versus the normal wild type PlyG, which yielded a very low colony forming unit percentage. This indicates that the cell-wall-binding domain of PlyG is essential for its catalytic activity, and that addition of PlyG restricts colonies of bacteria from forming, characterizing it as an endolysin with peptidoglycan catabolic process and cleavage. |
complete | ||||
|
enables |
GO:0008745 |
N-acetylmuramoyl-L-alanine amidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0009253 |
peptidoglycan catabolic process |
ECO:0000317 |
genomic context evidence used in manual assertion |
|
P |
The HHpred E-value is 3.5E^-25. The daughter cells in the paper require peptidoglycan catabolic process to separate. A fractured cell wall released lysosome and mutanolysin digestion. This related in the long amino acid chains breaking apart. |
complete | ||
|
involved_in |
GO:0009253 |
peptidoglycan catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
Contributes to |
GO:0008745 |
N-acetylmuramoyl-L-alanine amidase activity |
ECO:0000247 |
sequence alignment evidence used in manual assertion |
|
F |
Zinc binding and catalysis is highly conserved between Bacillus phages’ endolysins. This is indicated by the blue and red triangles located under the specific residues in the Figure 1. There is a high sequence alignment between PlyG and PlyLBa02 as shown by Figure 1 which is a sequence alignment diagram from ClustalX. PlyLBA02 and PlyG have a 93% identity in the enzymatic domain and a 60% identity in the C-terminal domain. Because of this similarity and the conserved residues, we can come to conclusion the PlyG is also involved in N-acetylmuramoyl-L-alanine amidase activity. |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Schuch, R et al. (2002) A bacteriolytic agent that detects and kills Bacillus anthracis. Nature 418 884-9 PubMed GONUTS page
- ↑ 2.0 2.1 Kikkawa, HS et al. (2008) Characterization of the catalytic activity of the gamma-phage lysin, PlyG, specific for Bacillus anthracis. FEMS Microbiol. Lett. 286 236-40 PubMed GONUTS page
- ↑ Arrigucci, R & Pozzi, G (2017) Identification of the chain-dispersing peptidoglycan hydrolase LytB of Streptococcus gordonii. PLoS ONE 12 e0176117 PubMed GONUTS page
- ↑ Jang, SY et al. (2017) Genome Characteristics of Lactobacillus fermentum strain JDFM216 for Application as Probiotic Bacteria. J. Microbiol. Biotechnol. PubMed GONUTS page
- ↑ Low, LY et al. (2005) Structure and lytic activity of a Bacillus anthracis prophage endolysin. J. Biol. Chem. 280 35433-9 PubMed GONUTS page
