BPP21:LYS

Species (Taxon ID)	Enterobacteria phage P21 (Bacteriophage 21) (Bacteriophage P21). (10711)
Gene Name(s)	R
Protein Name(s)	Lysozyme Endolysin Lysis protein Muramidase
External Links
UniProt	P27359
EMBL	M65239
PDB	3HDE 3HDF
PDBsum	3HDE 3HDF
ProteinModelPortal	P27359
SMR	P27359
CAZy	GH24
EvolutionaryTrace	P27359
GO	GO:0003796 GO:0016998 GO:0044659 GO:0042742 GO:0009253
CDD	cd00737
Gene3D	1.10.530.40
InterPro	IPR033907 IPR002196 IPR023346 IPR023347
Pfam	PF00959
SUPFAM	SSF53955

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0003796	lysozyme activity	PMID:19881499	ECO:0000315			F		Supplementary Figure 2. is a graph of results of an assay to determine lysozyme activity between purified full-length R^21 and truncated R^21. The truncated version has had the N-terminal SAR (signal anchor release) domain cleaved. Lyz^P1, a protein from phage P1 that had been previously determined to have lyzosyme activity, was included for comparison. The results found that the truncated version of R^21 did not produce any lysozyme activity, while the full-length version produced activity similar to Lyz^P1. The assay was done with the EnzChek® Lysozyme Assay which measures lysozyme activity on fluorescently-labeled Micrococcus lysodeikticus cell walls. When the fluorescently-labeled Micrococcus lysodeikticus cell walls are hydrolyzed, the fluorescein was released from the cell wall resulting in an increase in fluorescence. Trials with different concentrations of egg white lysozyme (EWL) (a standard for the EnzChek test) were run. The different shapes in the graph indicate EWL concentrations. Different line colors indicate which protein was being tested. In each trial, the full-length version of R^21 produced similar activity to Lyz^P1, while the truncated version of R^21 experienced almost total loss of function. These results support the idea that the SAR domain is necessary for and contributes to lysozyme activity in R^21.	complete CACAO 12587
Contributes to	GO:0003796	lysozyme activity	PMID:19881499	ECO:0000247		UniProtKB:Q37875	F		Figure 1a is a sequence alignment between R^21 Lyz^P1. Lyz^P1 is a previously researched protein that has lysozyme activity. The orange boxes have been identified as SAR domains, and in supplementary figure 2a are assayed to show the SAR domains are necessary for lysozyme activity. The yellow boxes are amino acid sequences that are inserted to produce chimeras for other tests. Alignment is inferred based on the E-8aa-(D/C)-5aa-T catalytic triad (blue and asterisks).	complete CACAO 12645
enables	GO:0003796	lysozyme activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002196 InterPro:IPR033907	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	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:0044659	cytolysis by virus of host cell	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033907	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: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-0326 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
involved_in	GO:0019835	cytolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0081	P		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
edit table

References

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