CAZyme Information: MGYG000002388_01283

Basic Information

• Species: Lacticaseibacillus paracasei
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus paracasei
• CAZyme ID: MGYG000002388_01283
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
388	MGYG000002388_1|CGC17	41803.9	8.8279

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002388	3076437	Isolate	China	Asia

• Gene Location: Start: 1244000; End: 1245166 Strand: +

Full Sequence      

MKLKTKLITLVVAFLAAISFALPSQVNAAKGDIGVDWAVYQGASGKYGTNNKFAIIQAGG
TQGGTLYDQWTYASQVKAAQANGLKAHTYLWYGVGGSADIGRQALDYFLPKILTPKGSIV
ALDYEDGASSSMAANTDAILYGMRRIAQAGYTPMYYSYKPYTLAHVDYQRILAEFPNSLW
IAAYPDYQIRALPDYGVFPSMPGIALYQFTSMHAAGGLDGNVDLLGVTDNGYSQQPVAPS
QPATPSQPSTSTAASDTDYAQTGVFKPSTTVNIRTGAGTGYTAVGSYVPGEILVYDHVYI
RGTYVWARYLSYSGRYHYVALGVNGGESYGSRSSGYTSPVSHTYYTVRSGDSFWSIASKY
GISMYTLAANNGKSIYSVIHPGESLYIR

Enzyme Prediction     

EC	3.2.1.17

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	35	217	3.7e-34	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06415	GH25_Cpl1-like	3.67e-66	32	225	1	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	1.13e-29	35	218	1	180	Glycosyl hydrolases family 25.
smart00641	Glyco_25	9.52e-23	116	231	1	109	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	7.07e-13	34	224	2	183	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.
cd00118	LysM	1.76e-11	343	387	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPC25929.1	9.73e-275	1	388	1	388
QPC28845.1	9.73e-275	1	388	1	388
AKU59311.1	9.73e-275	1	388	1	388
QJI66670.1	9.73e-275	1	388	1	388
QQX72097.1	8.19e-267	1	388	1	388

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1OBA_A	1.44e-22	30	211	4	178	ChainA, Lysozyme [Streptococcus phage Cp1]
1H09_A	1.94e-22	30	211	3	177	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXU_A	1.97e-22	30	211	4	178	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXV_A	5.02e-22	30	211	4	178	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	1.01e-38	30	225	152	343	D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2
P19385	1.81e-27	30	211	4	178	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2
P19386	1.04e-24	95	211	65	178	Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 PE=3 SV=1
P15057	1.08e-21	30	211	4	178	Lysozyme OS=Streptococcus phage Cp-1 OX=10747 GN=CPL1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000232	0.999109	0.000168	0.000187	0.000165	0.000148

TMHMM  Annotations     

start	end
7	29