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LAMBD:ENLYS

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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

PMID:28637001[4]

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
CACAO 13107

involved_in

GO:0044659

cytolysis by virus of host cell

PMID:6448076[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008933

lytic transglycosylase activity

PMID:10556513[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008933

lytic transglycosylase activity

PMID:9514719[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003796

lysozyme activity

PMID:4889461[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003796

lysozyme activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002196
InterPro:IPR034691

F

Seeded From UniProt

complete

involved_in

GO:0009253

peptidoglycan catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002196
InterPro:IPR034691

P

Seeded From UniProt

complete

involved_in

GO:0016998

cell wall macromolecule catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002196

P

Seeded From UniProt

complete

involved_in

GO:0019076

viral release from host cell

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR034691

P

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:IPR034691

P

Seeded From UniProt

complete

involved_in

GO:0009253

peptidoglycan catabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000433566

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000433566

F

Seeded From UniProt

complete

enables

GO:0003796

lysozyme activity

GO_REF:0000104

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

GO_REF:0000104

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

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0081

P

Seeded From UniProt

complete

part_of

GO:0030430

host cell cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1035
UniProtKB-SubCell:SL-0381

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-0081
UniProtKB-KW:KW-0204

P

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

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

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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. 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
  3. 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
  4. 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
  5. Bieńkowska-Szewczyk, K & Taylor, A (1980) Murein transglycosylase from phage lambda lysate. Purification and properties. Biochim. Biophys. Acta 615 489-96 PubMed GONUTS page
  6. 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