CAZyme Information: MGYG000002383_02084

Basic Information

• Species: Lacticaseibacillus zeae
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus zeae
• CAZyme ID: MGYG000002383_02084
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
323	MGYG000002383_14|CGC1	35455.73	9.2861

Genome Property

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

• Gene Location: Start: 2446; End: 3417 Strand: +

Full Sequence      

MSGPLTFLPIASAKAARKRVHSYIWYGVGASSQLGLEALDRYMPRIKAQTPKGSIVALDY
EDGASGNMAANTDAILAGMRRIRSEGYTPMYYSYKPYTLAHVDYQRILKEFPNSLWIAAY
RDYLPTTKPDYGYFPSMDGVAIWQYTSAFGLSQGLDGNIDLLGVADNGYSKQPVTPITPA
PSKPAQSTAATDTDYAQTGVFKPSTTVNIRTGAGTGYASVGSYAPGESVIYDHVYIRGTY
VWARYLSYSGRYHYVALGVNGGESYGSRSSNAQTYSHTYYTVRSGDSFWSIANKYGISMY
TLAVNNGKSIYSLIYPGESLYIR

Enzyme Prediction     

EC	3.2.1.17

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	10	148	4.5e-28	0.7288135593220338

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06415	GH25_Cpl1-like	4.65e-57	10	162	44	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.
smart00641	Glyco_25	4.21e-24	52	168	1	109	Glycosyl hydrolases family 25.
pfam01183	Glyco_hydro_25	1.80e-21	10	148	42	174	Glycosyl hydrolases family 25.
cd00118	LysM	4.19e-11	278	322	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.
cd00599	GH25_muramidase	2.38e-10	10	161	44	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUS98414.1	2.51e-235	1	323	1	323
AGP67429.1	2.51e-235	1	323	1	323
QPC13132.1	2.51e-235	1	323	1	323
QGV17231.1	2.51e-235	1	323	1	323
AWN82989.1	2.51e-235	1	323	1	323

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1H09_A	4.05e-24	56	147	88	177	ChainA, LYSOZYME [Streptococcus phage Cp1]
1OBA_A	4.11e-24	56	147	89	178	ChainA, Lysozyme [Streptococcus phage Cp1]
2IXU_A	4.11e-24	56	147	89	178	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXV_A	1.08e-23	56	147	89	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	2.72e-32	29	162	213	343	D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2
P19386	6.90e-27	56	175	89	198	Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 PE=3 SV=1
P19385	9.39e-25	9	147	44	178	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2
P15057	2.25e-23	56	147	89	178	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
1.000027	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002383_02084.