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BPPRD:ENLYS

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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

PMID:7925454[1]

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
CACAO 13267

involved_in

GO:0044277

cell wall disassembly

PMID:7925454[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0055036

virion membrane

PMID:11741849[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0051672

catabolism by organism of cell wall peptidoglycan in other organism

PMID:11741849[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051672

catabolism by organism of cell wall peptidoglycan in other organism

PMID:10931330[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003796

lysozyme activity

PMID:7925454[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003796

lysozyme activity

PMID:10931330[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0044659

cytolysis by virus of host cell

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016284

P

Seeded From UniProt

complete

enables

GO:0003796

lysozyme activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.2.1.17

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0016798

hydrolase activity, acting on glycosyl bonds

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0081
UniProtKB-KW:KW-0326

P

Seeded From UniProt

complete

part_of

GO:0019012

virion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0946

C

Seeded From UniProt

complete

involved_in

GO:0019835

cytolysis

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0204
UniProtKB-KW:KW-0081

P

Seeded From UniProt

complete

involved_in

GO:0042742

defense response to bacterium

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0081

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0081

F

Seeded From UniProt

complete

part_of

GO:0055036

virion membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0275

C

Seeded From UniProt

complete

GO:0044659

cytolysis by virus of host cell

PMID:16030234[4]

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. 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. 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. 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
  4. 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