CAZyme Information: MGYG000002388_00447

Basic Information

• Species: Lacticaseibacillus paracasei
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus paracasei
• CAZyme ID: MGYG000002388_00447
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
254	MGYG000002388_1|CGC4	27863.52	7.292

Genome Property

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

• Gene Location: Start: 456202; End: 456966 Strand: +

Full Sequence      

MAILMADVSSWQPESDSWFRKLADVGVKAVVVKLTEGTTYRNPKAAAQLAAGRRMGMQVH
GYHYAHYHNSADAVAEGRFFGTTAKALGLSTESVMAADVEDPGLSGELTGVTNVFLQTVK
AIGYPHTDLYTMASWLTARRFDRVALIPKNLWLASYGVNQPGVDNVGTWQFTNNFQGLGV
DMSYDFFGHYTTRLTGTLNGGVARVPTIRFHTVQPGESWWAIAHQYGHDMDKLAALNGKT
ILSVIHPGDQLRVE

Enzyme Prediction     

No EC number prediction in MGYG000002388_00447.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	7	177	3.3e-36	0.9717514124293786

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	4.66e-87	3	186	1	192	AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
pfam01183	Glyco_hydro_25	2.37e-34	7	180	2	180	Glycosyl hydrolases family 25.
cd06415	GH25_Cpl1-like	8.00e-34	7	181	5	190	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.
cd00599	GH25_muramidase	1.25e-27	7	172	4	169	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.
cd06525	GH25_Lyc-like	1.22e-20	7	174	4	169	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHQ64336.1	1.03e-188	1	254	1	254
QJI65895.1	1.03e-188	1	254	1	254
QPC25251.1	1.03e-188	1	254	1	254
CRL17016.1	1.03e-188	1	254	1	254
QDR75125.1	1.03e-188	1	254	1	254

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.07e-11	7	185	24	203	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.69e-11	7	185	24	203	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1H09_A	7.57e-09	22	174	22	178	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXU_A	7.59e-09	22	174	23	179	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXV_A	7.59e-09	22	174	23	179	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
P19385	6.37e-10	4	174	7	179	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2
P19386	2.83e-09	22	174	23	179	Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 PE=3 SV=1
P15057	4.16e-08	22	174	23	179	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
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002388_00447.