CAZyme Information: MGYG000001298_02014

Basic Information

• Species: Listeria grayi
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Listeriaceae; Listeria; Listeria grayi
• CAZyme ID: MGYG000001298_02014
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
328		36211.46	10.5549

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001298	2589961	Isolate	not provided	Europe

• Gene Location: Start: 498685; End: 499671 Strand: +

Full Sequence      

MGKIADISHHQGIVDWSKASKELDLAILRVQDGSNVADRQYKNNVAGAKKYGVPFGSYAF
TRFVSVADAKKEAQDFYNRSDKASKFWVADIEVKTMGDMAAGAKAFVGELRRLGAGKVGI
YIAHHLYNSLGINYKQFDFVWIPRYGNKPVYACDLWQHTSSGSLAGVNARVDLNTLNGSK
KLDWFIGATAKPSDDSHNSKPSTGKKLGKFKAGQKGVLSKNADRYATGEKIPTGVKNKAY
TVIQAKKEKHGSSSYKYLLKELNSWVWGADIKVQGASNSSKKEYYTVKSGDNLTAIAKKY
KTSVSKLRKLNKIKNPNLIKVGQKLRVK

Enzyme Prediction     

No EC number prediction in MGYG000001298_02014.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	167	4.6e-39	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06523	GH25_PlyB-like	1.46e-79	3	174	1	175	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd00599	GH25_muramidase	2.82e-34	3	174	1	184	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
cd06414	GH25_LytC-like	1.03e-29	3	174	2	188	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
COG3757	Acm	2.96e-22	3	180	64	257	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06413	GH25_muramidase_1	1.88e-18	6	178	7	191	Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBP06957.1	2.61e-107	1	327	1	311
AYV74335.1	1.41e-86	3	328	5	380
QKH60170.1	2.06e-86	3	327	4	326
ASL64938.1	1.28e-75	1	186	1	186
BAR87877.1	1.81e-75	1	188	1	187

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HMC_A	5.19e-74	1	185	4	188	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
2NW0_A	1.23e-71	2	187	1	185	ChainA, PlyB [Bacteriophage sp.],2NW0_B Chain B, PlyB [Bacteriophage sp.]
2WW5_A	6.32e-06	3	174	270	465	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	6.32e-06	3	174	270	465	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q5HGI5	5.44e-08	281	327	173	219	Probable cell wall hydrolase LytN OS=Staphylococcus aureus (strain COL) OX=93062 GN=lytN PE=3 SV=1
Q6G9W6	5.44e-08	281	327	173	219	Probable cell wall hydrolase LytN OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=lytN PE=3 SV=2
Q6GHI8	5.44e-08	281	327	173	219	Probable cell wall hydrolase LytN OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=lytN PE=3 SV=2
Q7A123	5.44e-08	281	327	173	219	Probable cell wall hydrolase LytN OS=Staphylococcus aureus (strain MW2) OX=196620 GN=lytN PE=3 SV=2
Q7A5Y8	5.44e-08	281	327	173	219	Probable cell wall hydrolase LytN OS=Staphylococcus aureus (strain N315) OX=158879 GN=lytN PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000022	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001298_02014.