9CAUD:B6SBV8

Species (Taxon ID)	Clostridium virus phiCD27. (559189)
Gene Name(s)	No Information Provided.
Protein Name(s)	Endolysin (ECO:0000313 with EMBL:ACH91325.1)
External Links
UniProt	B6SBV8
EMBL	EU719189
RefSeq	YP_002290910.1
PDB	3QAY 4CU5
PDBsum	3QAY 4CU5
SMR	B6SBV8
GeneID	6998161
KEGG	vg:6998161
KO	K01448
Proteomes	UP000001043
GO	GO:0046872 GO:0008745 GO:0009253
CDD	cd02696
Gene3D	3.40.630.40
InterPro	IPR002508
Pfam	PF01520
SMART	SM00646

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	PMID:21803993	ECO:0000315			F		Figures 2a and 2b shows the strain-specific, GFP-labeled, full-length protein as well as the N-terminus truncation of the full-length protein binding to the cell wall of C.difficile. Figure 2c shows the lytic activity of these two forms of CD27L against C. difficile cells compared to autolytic activity present in the buffer control. Figure 3 shows two residues, L130 and Y131, in the crystal structure of the catalytic domain of CD27L that are conserved for amidases specific to Clostridia. Figure 4 shows that there is a similar backbone structure between the N-terminus CD27L and another amidase, PlyPSA, specific to Listeria monocytogenes. A DALI analysis conducted by the authors reveals that the two structures are identical for 171 residues with a Z score of 24.2 indicating a strong structural match with an amidase protein. There is a 30% sequence identity and identical topologies between the catalytic domains of these two amidases. The structures differ in that the N-terminus of CD27L has larger loop extensions, and thereby larger substrate binding domain area, than PlyPSA. Figures 4b and 4c shows that the CD27L N-terminus surface is more positively charged than the surface of PlyPSA. However, these differences point to differences in substrate binding accessibility rather than differences in actual catalytic function. Figure 5 shows sequence homology between CD27L and 14 unique C. difficile-targeting endolysin proteins through a BLAST search. In addition figure 5 also shows that amongst these endolysin proteins the L130 and Y131 in the substrate binding domain of CD27L are conserved amongst the 14 unique proteins.	complete CACAO 12506
	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	PMID:21803993	ECO:0000315			F		Figures 1a, 1b, and 1c show how the lytic activity and specificity were effected by truncation. Figure 1a goes in depth on how the N- and C-terminal truncations of endolysin CD27L were produced as His-tagged proteins. Figure 1b displays the CD27L (1–179) and the full CD27L both failed to lyse C. tyrobutyricum. Figure 1c gives the assays of 10 the μg Ni-NTA-purified buffer incubated cells.	complete CACAO 12904
enables	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002508	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:IPR002508	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
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References

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