CAZyme Information: MGYG000002387_00315

Basic Information

• Species: Lactobacillus paragasseri
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus paragasseri
• CAZyme ID: MGYG000002387_00315
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
236	MGYG000002387_1|CGC3	27601.22	9.4114

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002387	2129154	Isolate	South Korea	Asia

• Gene Location: Start: 293759; End: 294469 Strand: -

Full Sequence      

MHRYRHKYTFPSIIILLILAFSGLVWGYFNMKQNTTVPRGSNMSVLGIELDQTKDYIDLH
KLEKNGISFVYLRSTQGKSYFDDNYLLYRDQLQGTNLNFGTIIAYSDETSNQDQYQYFVN
KVGTNTGSLPVMIVPATNHLTKSYWKKMGEFAQMINNLGKRTMIAGDYHYHNYFPEGTRF
LYTGASLKDRRHYAFWCYTQNGRVKNIDNLDRDVTMFAYIGTNTQYAQLYSQEKTQ

Enzyme Prediction     

No EC number prediction in MGYG000002387_00315.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	54	205	2.4e-21	0.9491525423728814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06419	GH25_muramidase_2	8.22e-71	38	212	1	184	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.
cd00599	GH25_muramidase	3.98e-12	47	214	2	185	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.
cd06413	GH25_muramidase_1	2.44e-07	57	214	15	188	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.
cd06525	GH25_Lyc-like	0.002	47	143	2	99	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has 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.
smart00641	Glyco_25	0.004	45	123	1	81	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBD48239.1	9.86e-178	1	236	1	236
VEF35076.1	2.83e-177	1	236	1	236
ART97683.1	4.32e-177	1	236	3	238
QTP20164.1	4.32e-177	1	236	3	238
QHC52819.1	4.32e-177	1	236	3	238

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.02e-08	45	226	16	213	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.999413	0.000344	0.000110	0.000003	0.000001	0.000166

TMHMM  Annotations     

start	end
7	29