BACAN:Q81WA9

Species (Taxon ID)	Bacillus anthracis. (1392)
Gene Name(s)	cwlA (ECO:0000313 with EMBL:BAR75273.1)
Protein Name(s)	N-acetylmuramoyl-L-alanine amidase (ECO:0000313 with EMBL:ALC35984.1) N-acetylmuramoyl-L-alanine amidase CwlA (ECO:0000313 with EMBL:BAR75273.1) N-acetylmuramoyl-L-alanine amidase family protein (ECO:0000313 with EMBL:AJH88538.1) Prophage LambdaBa02, N-acetylmuramoyl-L-alanine amidase, family 2 (ECO:0000313 with EMBL:AAT33191.1)
External Links
UniProt	Q81WA9
EMBL	AE017334 CP009902 CP012519 AP014833 LFYJ01000068 LFYH01000003 LFYG01000012 LFYI01000025 LFYF01000022 LGIE01000010 LGIG01000014 LGID01000085 LHUN01000026 LHUO01000006
RefSeq	WP_000405801.1
PDB	1YB0 2AR3
PDBsum	1YB0 2AR3
STRING	198094.BA_4073
DNASU	1087444
EnsemblBacteria	AAT33191 AJG30579 AJH88538
KEGG	banh:HYU01_19915 bar:GBAA_4073
eggNOG	ENOG4105T4X COG5632
HOGENOM	HOG000273688
KO	K01447
OMA	DENGWHA
OrthoDB	EOG6W19KX
BioCyc	BANT260799:GJAJ-3842-MONOMER BANT261594:GJ7F-3960-MONOMER
Proteomes	UP000000594 UP000031920 UP000036891 UP000037044 UP000037060 UP000037079 UP000037132 UP000037296 UP000037367 UP000037383 UP000037483 UP000037502
GO	GO:0046872 GO:0008745 GO:0009253
Gene3D	3.40.80.10
InterPro	IPR021976 IPR002502
Pfam	PF12123 PF01510
SMART	SM00644
SUPFAM	SSF55846

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:16103125	ECO:0000314			F		PlyL is an endolysin enzyme with 2 separate domains, an N-terminal catalytic domain, and a C-terminal cell wall binding domain. This annotation is for the N-terminal domain of PlyL. Peptidoglycan from B. subtilis was subjected to both the full-length PlyL and the N-terminal domain only. In supplemental figure 1, (see link: http://www.jbc.org/content/suppl/2005/08/16/M502723200.DC1/Suppdata.pdf) the amount of 2,4-dinitrophenyl-alanine is shown to increase sharply, indicating that PlyL is an N-acetylmuramoyl-L-alanine amidase. Additionally, the figure shows that alanine is increased even more when the N-terminal domain alone is used, compared to the full-length protein. As additional support that PlyL is an amidase, figure 2 compares the crystal structure of PlyL to other known amidase enzymes. Figure 4 shows a time course assay where the purified endolysin (PlyL) was able to lyse 4 different bacillus species cultures within 400 seconds. In 4a, the lysing capabilities of the full-length version of PlyL are shown. In 4b, the lysing capabilities of the N-terminal portion only are shown. The N-terminal domain by itself is more effective at cleaving Bacillus species than the entirety of PlyL.	complete CACAO 11527
	GO:0051672	catabolism by organism of cell wall peptidoglycan in other organism	PMID:16103125	ECO:0000314			P		Peptidoglycan from B. subtilis was subjected to both the full-length PlyL and the N-terminal domain only. In supplemental figure 1, (see link: http://www.jbc.org/content/suppl/2005/08/16/M502723200.DC1/Suppdata.pdf) the amount of 2,4-dinitrophenyl-alanine is shown to increase sharply, indicating that PlyL is an N-acetylmuramoyl-L-alanine amidase. Additionally, the figure shows that alanine is increased even more when the N-terminal domain alone is used, compared to the full-length protein.	complete CACAO 11533
Contributes to	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	PMID:16103125	ECO:0000247		UniProtKB:Q8LTE6	F		Zinc binding and catalysis is highly conserved between Bacillus phages. There is a high sequence alignment between PlyLBa02 and PlyG as shown by Figure 1 which is a sequence alignment diagram from ClustalX. PlyG and PlyLBA02 have a 93% identity in the enzymatic domain and a 60% identity in the C-terminal domain. Because of this similarity, we can come to conclusion the PlylBa02 is also involved in N-acetylmuramoyl-L-alanine amidase activity.	complete CACAO 12461
Contributes to	GO:0019835	cytolysis	PMID:16103125	ECO:0000315			P		In Figure 4, an assay of lytic enzyme activity of PlyL and its mutant, Ply21 was conducted on the cell wall of five bacterial hosts. The mutant Ply21 is described as the full-length protein of PlyL with the removal of the C-terminal domain involved in cell wall binding, leaving behind only the presence of the N-terminal catalytic domain. In Panel B, the lysing abilities of Ply21 are shown, and the removal of the C-terminal cell wall binding domain did not have a significant effect on the lysing of the bacterial hosts. However, the N-terminal catalytic domain displayed a higher percent absorbance over time as compared to Panel A, (which displayed the lysing abilities of the full length protein). Furthermore, B. subtilis (yellow-orange line) displayed the highest lysing ability than all of the bacterial hosts, with the absorbance rate being higher in the graph of Panel B than Panel A. This concludes that the mutant PlyL 21, also known as the N-terminal catalytic domain of the full length PlyL protein with the C-terminal binding domain removed, is most efficient in cytolysis and that the removal of the C-terminal cell wall binding domain does not inhibit nor improve the lysing ability of PlyL on the cell wall of bacterial hosts.	complete CACAO 12907
Contributes to	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	PMID:16103125	ECO:0000255		UniProtKB:0008745	F		Figure 5 shows that catalytic activity of N-terminal domain binding to the C-terminal domain in which it shows the C-terminal domain to catalyze the cell wall component. This proves that the N-acetylmuramoyl-L-alanine amidase activity is being used.	complete CACAO 12910
enables	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002502 InterPro:IPR036505	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:IPR002502 InterPro:IPR036505	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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