GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
BPPRD:ENLYS
Contents
Species (Taxon ID) | Enterobacteria phage PRD1 (Bacteriophage PRD1). (10658) | |
Gene Name(s) | XV | |
Protein Name(s) | Endolysin
Beta-1,4-N-acetylmuramidase Lysozyme Lytic enzyme Muramidase Protein P15 | |
External Links | ||
UniProt | P13559 | |
EMBL | X14980 M22161 AY848689 | |
PIR | S03568 | |
RefSeq | NP_040683.1 | |
SMR | P13559 | |
GeneID | 1260935 | |
KEGG | vg:1260935 | |
Proteomes | UP000002143 | |
GO | GO:0055036 GO:0003796 GO:0051672 GO:0044277 GO:0019835 GO:0044659 GO:0042742 | |
InterPro | IPR024408 IPR016284 | |
Pfam | PF11860 | |
PIRSF | PIRSF001069 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0033922 |
peptidoglycan beta-N-acetylmuramidase activity |
ECO:0000314 |
F |
In figure 3, samples of cell walls were combined with the enzyme P15, hydrolyzed with HCl, and chromatographed on a column. Eluted fractions were then tested for radioactivity. Only the sample with [3H]muramicitol was seen only in the tubes with P15 and cell walls, not in any of the control. This meant that P15 bound to [3H]muramicitol and hydrolyzed it, which would lead to cell death. It had previously been discovered that adding p15 to a tube of E. coli would decrease the turbidity of the tube by killing the cells. Figure 3 was just to show the nature of the cells' death. |
complete | |||||
involved_in |
GO:0044277 |
cell wall disassembly |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0055036 |
virion membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0044659 |
obsolete catabolism by organism of cell wall peptidoglycan in other organism |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0044659 |
viral release from host cell by cytolysis |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
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:0000314 |
direct assay evidence used in manual assertion |
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 |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0003796 |
lysozyme activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016798 |
hydrolase activity, acting on glycosyl bonds |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
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 | |||
part_of |
GO:0019012 |
virion |
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:0042742 |
defense response to bacterium |
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 | |||
part_of |
GO:0055036 |
virion membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
GO:0044659 |
cytolysis by virus of host cell |
ECO:0006006 |
P |
Figure 5 shows the electrochemical assays performed on recombinant E. coli to determine the physiological effects of PRD1 endolysin (pMG118) involved in viral cytolysis. Host cell permeability (K+ and TPP+), cell growth and cell cytolysis (A550) were measured. Fig. 5a exhibited cell growth that steadily increased but never decreased, and variable changes in permeability. There was a peaked influx and efflux of K+, a decrease in TPP+, and steady, increased A550. The absence of endolysin and the presence of holin (pGZ9) failed to rupture cell membrane. Fig. 5e exhibited cytolysis with co-expressed holin and endolysin. Permeability and cell growth increased and peaked, but decreased dramatically below the initial baseline. The initial influx and latter efflux of K+, TPP+, and A550 values displayed how endolysin works to rupture host membrane when simultaneously present with holin in PRD1 for this synergistic effect. |
complete | |||||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 Caldentey, J et al. (1994) Gene XV of bacteriophage PRD1 encodes a lytic enzyme with muramidase activity. Eur. J. Biochem. 225 341-6 PubMed GONUTS page
- ↑ 2.0 2.1 Rydman, PS & Bamford, DH (2002) The lytic enzyme of bacteriophage PRD1 is associated with the viral membrane. J. Bacteriol. 184 104-10 PubMed GONUTS page
- ↑ 3.0 3.1 Rydman, PS & Bamford, DH (2000) Bacteriophage PRD1 DNA entry uses a viral membrane-associated transglycosylase activity. Mol. Microbiol. 37 356-63 PubMed GONUTS page
- ↑ Ziedaite, G et al. (2005) The Holin protein of bacteriophage PRD1 forms a pore for small-molecule and endolysin translocation. J. Bacteriol. 187 5397-405 PubMed GONUTS page