BPMD2:LYSB

Species (Taxon ID)	Mycobacterium phage D29 (Mycobacteriophage D29). (28369)
Gene Name(s)	12
Protein Name(s)	Endolysin B (ECO:0000303 with PMID:19555454) Gene 12 protein (ECO:0000305) Gp12 (ECO:0000305) Mycolylarabinogalactan esterase (ECO:0000303 with PMID:19555454)
External Links
UniProt	O64205
EMBL	AF022214
PIR	A72801
RefSeq	NP_046827.1
PDB	3HC7
PDBsum	3HC7
ProteinModelPortal	O64205
SMR	O64205
ESTHER	bpmd2-vg12
GeneID	1261627
KEGG	vg:1261627
OrthoDB	VOG090000F7
EvolutionaryTrace	O64205
Proteomes	UP000002131
GO	GO:0016787 GO:0044659 GO:0042742 GO:0008152
Gene3D	3.40.50.1820
InterPro	IPR029058 IPR000675
Pfam	PF01083
SUPFAM	SSF53474

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
Contributes to	GO:0044659	cytolysis by virus of host cell	other:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2774421/figure/F3/	ECO:0000255		PMID:https	P		Of the 253 residue for D29 LysB, 170 are typical for the homologic match to the alpha/beta hydrolase. this structure is composed of a beta sheet in between 2 alpha sheets. The remaining 81- residues form a C-terminal alpha helix that has a backside attachment to the Beta sheet. the structure and polarization of the end of the C-terminal yields a structure where Gly117-ASN118-PRO119 allowing a 180 degree turn underneath ASP 166 with 117 and 119 forming hydrogen bonds with met120, Arg121, and Asp160 allowing rotation that helps facilitate the catalytic state of the release of mycolic acid from the host cell membrane. The composition of the residues leads a 21% identity with amino acids. However, it yields a high Z-score of 20.3 for comparison in Dali. This lack of identity is possibly due to the 55 residues that are high in glycine residues that lead to the structure in between the second and third helices.	complete CACAO 12629
Contributes to	GO:0044659	cytolysis by virus of host cell	PMID:19555454	ECO:0000316		PMID:https	P		Figure 4- After determining if M. smegmatis is an appropriate target host cell and it's mycolyl-arabinogalactan-peptidoglycan membrane is hydrolyzed, testing the proposed function of a Serine esterase was tested by Chromatography to determine the release of Mycolic acids. Each time period is noted in figure A. Figure A and B are time and concentration dependent of the release of lipids. This is designed to mock the mycolic acid release known from treating the membrane with tetrabutylammonium. Figure C is classifying the concentration of the specific lipids released in figure A and B. Figure D is the most critical, by measuring the mutant that had the serine 82 residue removed, an important catalyst, along with test of other chemicals and controls, it is evident that Lyse B intact with the Serine and other catalysts intact are essential to releasing the free mycolic acids in the cell membrane.	complete CACAO 12921
	GO:0016787	hydrolase activity	PMID:19555454	ECO:0000314			F		The protein LysB from mycobacteriophage D29 was expressed (and also purified) using the plasmid pLAM3, with its molecular weight being around 30kDa (Fig. 2A). This purified LysB protein was used to measure LysB ability to perform hydrolysis of p-nitrophenyl butyrate (pNPB), in which it releases p-nitrophenol. A specific activity of 0.72 U/mg was measured for D29 LysB (Fig. 2B). This number was much higher than 0.12 U/mg, which was measured for a similar protein, Ms6 LysB. Lypolytic activity also decreased as D29 LysB had longer substrates (Fig. 2B).	complete CACAO 13275
involved_in	GO:0044659	cytolysis by virus of host cell	PMID:19555454	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000675	F		Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	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
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
involved_in	GO:0019835	cytolysis	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0081 UniProtKB-KW:KW-0204	P		Seeded From UniProt	complete
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References

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