CAZyme Information: MGYG000002384_00572

Basic Information

• Species: Lactobacillus helveticus
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus helveticus
• CAZyme ID: MGYG000002384_00572
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
225		24194.34	9.9079

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002384	2058319	Isolate	Russia	Europe

• Gene Location: Start: 515789; End: 516466 Strand: +

Full Sequence      

MTPMGYHFATFSSNASLAKSEAKYAVSSAKALGLPKGSYLACDYETVSGNIITNGKNVTA
KAILAFMDEIKAAGYQPLLYASSSVLQNNINTPSIVKKYPNSLWVAAYAISGRVDKPNFK
YFPSMDGIAIWQYTDNWKGMSTDGNVTILPLSISGSAVSQAPSNSNTKHTGTSKSYVYDG
NGKRTGEVYKAYVSVTYYGGKTKLSNGKSAVKIGDNKYTSWQVIS

Enzyme Prediction     

EC	3.2.1.17

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	4	138	2.8e-28	0.6779661016949152

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06415	GH25_Cpl1-like	8.89e-60	1	149	52	196	Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage.
pfam01183	Glyco_hydro_25	2.74e-20	6	136	55	174	Glycosyl hydrolases family 25.
smart00641	Glyco_25	2.02e-19	36	146	1	100	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	3.21e-16	6	146	57	181	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	4.66e-15	6	148	61	187	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADQ59232.1	1.38e-132	1	218	95	314
AUX15893.1	1.38e-132	1	218	95	314
ADZ07348.1	1.38e-132	1	218	95	314
ATO52288.1	1.43e-132	1	218	96	315
QDD70318.1	1.43e-132	1	218	96	315

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1H09_A	1.35e-18	3	149	54	187	ChainA, LYSOZYME [Streptococcus phage Cp1]
1OBA_A	1.36e-18	3	149	55	188	ChainA, Lysozyme [Streptococcus phage Cp1]
2IXU_A	1.36e-18	3	149	55	188	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXV_A	3.54e-18	3	149	55	188	ChainA, LYSOZYME [Streptococcus phage Cp1],2J8F_A Chain A, LYSOZYME [Streptococcus phage Cp1],2J8G_A Chain A, LYSOZYME [Streptococcus phage Cp1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8HA43	6.80e-23	3	149	203	343	D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2
P33486	8.42e-22	10	127	64	181	Lysozyme OS=Lactococcus phage mv1 OX=33769 GN=lysA PE=1 SV=3
P19385	1.12e-18	3	149	55	188	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2
P19386	2.07e-18	2	149	54	188	Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 PE=3 SV=1
P15057	7.44e-18	3	149	55	188	Lysozyme OS=Streptococcus phage Cp-1 OX=10747 GN=CPL1 PE=1 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
1.000080	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002384_00572.