BPA50:AEPE

Species (Taxon ID)	Listeria phage A500 (Bacteriophage A500). (40522)
Gene Name(s)	ply (synonyms: ply500)
Protein Name(s)	L-alanyl-D-glutamate peptidase
External Links
UniProt	Q37979
EMBL	X85009
PIR	S69801
RefSeq	YP_001468411.1
PDB	2VO9
PDBsum	2VO9
ProteinModelPortal	Q37979
SMR	Q37979
MEROPS	M15.021
GeneID	5601386
KEGG	vg:5601386
KO	K17733
EvolutionaryTrace	Q37979
GO	GO:0005576 GO:0016787 GO:0071555
Gene3D	3.30.1380.10
InterPro	IPR009045
SUPFAM	SSF55166

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
Contributes to	GO:0016787	hydrolase activity	PMID:18560152	ECO:0000247		UniProtKB:Q37976	F		The N-terminal enzymatically active domain (EAD) of an endolysin is the source of it's catalytic behavior, and in this sense, will determine evidence of hydrolytic activity. Endolysin PLY500 has displayed L-alanoyl-D-glutamate endopeptidase activity in Listeria phages. Listeria phage PLY118 (Listeria phage A118) shows 30% amino acid alignment with PLY500 in terms of EAD (fig.1, indicated by overhead black bars). While there is no relations between the C-terminal domains (structural evidence) of PLY500 and PLY118, the genes active in binding the catalytic Zn2+ ion and LAS protein identification are conserved within this 30% PLY118 matching amino acid sequence. From this information it is likely that the N-terminal domains of PLY118 and PLY500 are similar enough to be classified in the same functional LAS family.	complete CACAO 12475
	GO:0016787	hydrolase activity	PMID:8577256	ECO:0000247		PMID:8577256	F		Fig.3 shows high similarity between ply118 and ply500 protein sequence. wither it's a identical residue or a conservative substitution, the two enzymes share the acceptable shared identity	complete CACAO 12491
	GO:0071555	cell wall organization	PMID:18560152	ECO:0000314			P		Figure 1 of the paper compares proteins PLY500 and PLY118. According to the introduction of the paper PLY500 is an endolysin that consists of a C-terminal cell wall binding domain and a N-terminal enzymatically active domain (EAD). The cell wall binding domain is for recognizing and binding to specific bacterial cell surfaces. PLY118 is another protein from a related Listeria phage, A118. PLY118 is a peptidase in A118. Both of these proteins have unrelated cell wall binding domains but their endopeptidase has a clear sequence homology to EAD500. EAD500 was recently shown to be chromosomally encoded in Bacillus subtilis.	complete CACAO 12635
	GO:0016787	hydrolase activity	PMID:8577256	ECO:0000314			F		In fig.8, an optical density assay was performed on Listeria monocytogenes WSLC 1001. the assay shows a decrees in the optical density of L.monocytogenes cell wall after being exposed to PL118 (closed circles). PL118 and PL500 have acceptable sequence similarity to assume they have the same lytic function. the control(open circles) shows no effect on the cell wall without the addition of PL118.	complete CACAO 12677
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0008233	P		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR039561	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
involved_in	GO:0071555	cell wall organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0961	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
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References

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