CAZyme Information: MGYG000002774_02310

Basic Information

• Species: Schleiferilactobacillus harbinensis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Schleiferilactobacillus; Schleiferilactobacillus harbinensis
• CAZyme ID: MGYG000002774_02310
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
249	MGYG000002774_11|CGC3	27405.25	9.9432

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002774	3078759	MAG	United States	North America

• Gene Location: Start: 102214; End: 102963 Strand: -

Full Sequence      

MRRPDPIYTNTFRRHWVWWLLLLVAVIIAGVLAWRYFAPVDLTRGEYPVNGTLVSQEDGT
IDFPSLKKAGARFAYIHAAQGASYQDDRVGENLASAQGAQLAVGVEHALSFDTTPAAQMA
NLTKAVAGNWGNLPVAVTLSLYGTYESTPPDKARVAALLNSMQSLLQKNGRSMIVRTTTE
LADRYALTGHYALWYSDAQTAAKTVLFVQRGKFPHNTALPLVTFNGDRTRWQQQFHVTLT
ALALAGARP

Enzyme Prediction     

No EC number prediction in MGYG000002774_02310.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	54	200	3.2e-22	0.8305084745762712

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06419	GH25_muramidase_2	1.56e-37	47	224	6	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	1.25e-18	47	194	1	150	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	5.74e-18	51	197	2	148	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.
pfam01183	Glyco_hydro_25	3.92e-10	54	194	3	148	Glycosyl hydrolases family 25.
cd06412	GH25_CH-type	2.34e-08	49	130	1	82	CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFR62539.1	1.39e-179	1	249	1	249
QEU46964.1	8.06e-179	1	249	1	249
QFR24006.1	8.06e-179	1	249	1	249
QEU39092.1	2.47e-35	1	231	1	247
QIR09946.1	2.47e-35	1	231	1	247

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	1.54e-06	49	130	5	86	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	7.11e-06	35	130	72	163	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

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
1.000040	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
16	38