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LAMBD:ENLYS
Contents
Species (Taxon ID) | Escherichia phage lambda (Bacteriophage lambda). (10710) | |
Gene Name(s) | R | |
Protein Name(s) | Endolysin (ECO:0000255 with HAMAP-Rule:MF_04109, ECO:0000303 with Ref.2)
Lysis protein (ECO:0000255 with HAMAP-Rule:MF_04109) Lysozyme (ECO:0000255 with HAMAP-Rule:MF_04109, ECO:0000303 with PMID:10556513[1], ECO:0000303 with PMID:4889461[2]) Transglycosylase (ECO:0000255 with HAMAP-Rule:MF_04109, ECO:0000303 with PMID:6460914[3]) | |
External Links | ||
UniProt | P03706 | |
EMBL | J02459 | |
PIR | B04333 | |
RefSeq | NP_040645.1 | |
PDB | 1AM7 1D9U 3D3D | |
PDBsum | 1AM7 1D9U 3D3D | |
ProteinModelPortal | P03706 | |
SMR | P03706 | |
IntAct | P03706 | |
DrugBank | DB02325 | |
CAZy | GH104 | |
GeneID | 2703480 | |
KEGG | vg:2703480 | |
OrthoDB | VOG090000W9 | |
EvolutionaryTrace | P03706 | |
Proteomes | UP000001711 | |
GO | GO:0030430 GO:0052764 GO:0052762 GO:0003796 GO:0016998 GO:0044659 GO:0042742 GO:0009253 | |
HAMAP | MF_04109 | |
InterPro | IPR002196 IPR023346 | |
Pfam | PF00959 | |
SUPFAM | SSF53955 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0044659 |
cytolysis by virus of host cell |
ECO:0000314 |
P |
The R lysis cassette, including R endolysin and S holin genes was synthesized and inserted into a plasmid under regulation of arabinose and temperature sensitive promoters. The plasmid was introduced into Δasd E. coli χ6212 and the construct was named JOL1675. Under conditions inducing expression of the plasmid, presence of the R endolysin was confirmed by Western Blot and shown in Figure 2. A band at 17.7 kDa, the estimated size of the endolysin, was seen in cells with the plasmid expressed, but not in cells grown under conditions repressing expression. Lysis efficiency was confirmed by monitoring the number of viable cells, which declined to 0 after 48 hours of lysis, as shown in Figure 4. No viable cells remained, indicating that the endolysin effectively ruptured and killed the hosts. |
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 | |||
enables |
GO:0008933 |
lytic transglycosylase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008933 |
lytic transglycosylase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003796 |
lysozyme activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003796 |
lysozyme activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009253 |
peptidoglycan catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0016998 |
cell wall macromolecule catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0019076 |
viral release from host cell |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0044659 |
cytolysis by virus of host cell |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009253 |
peptidoglycan catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000433566 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0016829 |
lyase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000433566 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0003796 |
lysozyme activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000433566 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0044659 |
cytolysis by virus of host cell |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000433566 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0042742 |
defense response to bacterium |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0030430 |
host cell cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0019835 |
cytolysis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0008152 |
metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0003824 |
catalytic activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Evrard, C et al. (1999) Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme. FEBS Lett. 460 442-6 PubMed GONUTS page
- ↑ 2.0 2.1 Black, LW & Hogness, DS (1969) The lysozyme of bacteriophage lambda. I. Purification and molecular weight. J. Biol. Chem. 244 1968-75 PubMed GONUTS page
- ↑ Bienkowska-Szewczyk, K et al. (1981) The R gene product of bacteriophage lambda is the murein transglycosylase. Mol. Gen. Genet. 184 111-4 PubMed GONUTS page
- ↑ Won, G et al. (2017) A novel method to generate Salmonella Typhi Ty21a ghosts exploiting the λ phage holin-endolysin system. Oncotarget 8 48186-48195 PubMed GONUTS page
- ↑ Bieńkowska-Szewczyk, K & Taylor, A (1980) Murein transglycosylase from phage lambda lysate. Purification and properties. Biochim. Biophys. Acta 615 489-96 PubMed GONUTS page
- ↑ Evrard, C et al. (1998) Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes. J. Mol. Biol. 276 151-64 PubMed GONUTS page