CAZyme Information: MGYG000000843_01713

Basic Information

• Species: Lacticaseibacillus sp900540605
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus sp900540605
• CAZyme ID: MGYG000000843_01713
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
389		42248.18	10.4169

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000843	2470970	MAG	China	Asia

• Gene Location: Start: 166; End: 1335 Strand: +

Full Sequence      

MIGRFIKAIMVSKAVIAQVGGTYNGLYVVQSTYRTQVSSAIAAGKHAHTYIWYQVGGSIP
VAKAAMDKFLPMVQTPKGSIVALDYEAGASGNKQANTNAIIYGLQRVKAAGYTPVLYSGK
YYLNDHTYYSQINKAFPTSLWIASYPTTRTVTAPNFNYFPSMDGINMWQFTDAYSTPGLD
ASVDLTGITDNGYGRSTTTDTGKVIVKPNTKTPATNAGQSANNTHKSSISTGYAVKVNLR
AKRYANGVAIPNWVKGRTYKVIQTSGNKVLLGSIMSWVNRSDVEILQTSSQAKSTQTSKL
SVDGIWGKATTKALQRHEGTPVDGVISYNSQLVRAMQRHLGVTVDGIMGHKTIRAMQRHL
GTPVDGVISYHSRMVMAMQQRLNSGTLPF

Enzyme Prediction     

EC	3.2.1.17

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	14	179	1e-33	0.8757062146892656

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06415	GH25_Cpl1-like	2.03e-64	13	186	23	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	6.42e-31	25	179	30	180	Glycosyl hydrolases family 25.
smart00641	Glyco_25	2.91e-24	77	192	1	109	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	2.19e-12	25	185	32	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.
cd06414	GH25_LytC-like	1.23e-10	13	185	24	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
BAN73998.1	6.95e-207	12	389	52	440
QPC16279.1	6.95e-207	12	389	52	440
QFG46764.1	4.80e-115	13	329	57	368
ANT43548.1	5.35e-107	13	343	51	383
ARE11857.1	7.57e-107	13	297	51	332

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1H09_A	1.33e-19	50	171	58	176	ChainA, LYSOZYME [Streptococcus phage Cp1]
1OBA_A	1.35e-19	50	171	59	177	ChainA, Lysozyme [Streptococcus phage Cp1]
2IXU_A	1.35e-19	50	171	59	177	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXV_A	3.40e-19	50	171	59	177	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	1.47e-24	50	185	207	342	D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2
P19386	8.52e-20	15	171	22	177	Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 PE=3 SV=1
P15057	7.39e-19	50	171	59	177	Lysozyme OS=Streptococcus phage Cp-1 OX=10747 GN=CPL1 PE=1 SV=2
P19385	8.88e-18	50	171	61	177	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2
P33486	1.95e-11	56	164	66	181	Lysozyme OS=Lactococcus phage mv1 OX=33769 GN=lysA PE=1 SV=3

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
0.967672	0.031978	0.000250	0.000052	0.000028	0.000057

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000843_01713.