CAZyme Information: MGYG000002383_00628

Basic Information

• Species: Lacticaseibacillus zeae
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus zeae
• CAZyme ID: MGYG000002383_00628
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
241		27591.37	10.1797

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002383	3001027	Isolate	Italy	Europe

• Gene Location: Start: 145335; End: 146060 Strand: +

Full Sequence      

MRSRRVIYADTYRHRWHRWLFIASGILAVLLLVGWWLQRNPRPDPATYPILGVRLDQTDG
IQDFDRLRASKVSFVYLKATEGSSYFDDNFNTNFDQAAGSRLSIGVYHVFSFETTPQAQA
LQFERKVGSNIGDLPIGIYLSYYREEKPSAAWLTQHLTTFITLIQQQYHRPVLLMGSPEI
LKAVKTVASHAPRWIDSDQRPTGSGNFWQYTDGARIPNGPQAAYRAAVFMGKRSSFLRLA
Q

Enzyme Prediction     

No EC number prediction in MGYG000002383_00628.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	59	217	1.8e-29	0.9491525423728814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06419	GH25_muramidase_2	1.62e-86	43	229	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.
cd00599	GH25_muramidase	2.86e-32	52	219	2	177	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	7.80e-25	48	217	1	178	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.
pfam01183	Glyco_hydro_25	2.47e-17	59	217	7	178	Glycosyl hydrolases family 25.
COG3757	Acm	2.48e-16	41	217	53	242	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVI32976.1	1.04e-161	1	241	1	241
QXG59944.1	2.10e-161	1	241	1	241
QVI38130.1	2.10e-161	1	241	1	241
ARY91147.1	8.21e-159	1	241	1	241
QPC17365.1	3.34e-158	1	241	1	241

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	2.55e-20	48	236	14	213	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	6.49e-06	47	108	2	63	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

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
1.000033	0.000008	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
20	37