CAZyme Information: MGYG000004860_00649

Basic Information

• Species: Levilactobacillus namurensis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Levilactobacillus; Levilactobacillus namurensis
• CAZyme ID: MGYG000004860_00649
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
255	MGYG000004860_4|CGC1	29137.6	9.9046

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004860	2610545	MAG	China	Asia

• Gene Location: Start: 3509; End: 4276 Strand: -

Full Sequence      

MRRRDYQPIYEDTFRRRRRWHRVVVLLIALLLGGFGTWGWHQWQQYHAAQLAQFPVRGVS
INQDSGYLDFQQLAKHHQFVYLQATSGATYSDDDFSNNYSRSQGASMKVGVVHTFSFTSS
AKRQYAHFSQIVGNETGTLPIVVNVAYYDQFNSDNQSMAKQGQKLKALVTRLENTYQQGV
IIQAKQAVLTQFVRPALPHQAEWVVDGKLQHYASPVQLIEYDATGRLTQSGQSQAVGLSV
FNGTRRQWATFSHDD

Enzyme Prediction     

No EC number prediction in MGYG000004860_00649.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	62	205	2.9e-23	0.8022598870056498

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06419	GH25_muramidase_2	5.02e-63	49	241	1	190	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.
cd06413	GH25_muramidase_1	3.29e-24	54	243	1	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.
cd00599	GH25_muramidase	4.60e-19	57	193	1	134	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.
COG3757	Acm	8.32e-11	51	251	58	263	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06525	GH25_Lyc-like	1.15e-10	57	128	1	73	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFR61107.1	6.55e-126	1	255	1	255
SMS13877.1	7.28e-126	1	255	4	258
QMU07289.1	2.82e-106	1	255	2	256
AKP65411.1	7.27e-101	1	252	1	251
ARN89745.1	8.70e-100	3	253	4	253

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	9.35e-19	53	255	13	220	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
0.998574	0.000389	0.000176	0.000002	0.000001	0.000881

TMHMM  Annotations     

start	end
20	42