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LAMBD:LYS
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 |
|---|---|---|---|---|---|---|---|---|---|---|
|
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
- ↑ 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
