CAZyme Information: MGYG000004860_00576

Basic Information

• Species: Levilactobacillus namurensis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Levilactobacillus; Levilactobacillus namurensis
• CAZyme ID: MGYG000004860_00576
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
398	MGYG000004860_3|CGC3	44280.34	10.1114

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004860	2610545	MAG	China	Asia

• Gene Location: Start: 94658; End: 95854 Strand: -

Full Sequence      

MFKNHHRFGHRVFQTAAMVGALAGLAWGSQTVAHASTLAVPDISEWQGRLSAGEVAGLKN
QVSFVINRRQYGVGYQDLYATNNTNLYVRYGVPFGEYDYARFHDAASARQEAQDFYARSN
KHANFYVLDFEENDVTSGSTNAAVRAWADEMRSLTTKHLVFYSYQSFATTYANSARKAFD
AQWIANYSSTPTIPFALWQYTDHNYLSALGQYTDNSRVTTSVHPVSWWADSAALALTHAP
ATSSATTPPTNTNVNPTVAAPSTSGTGSTFTGYPVGAYAELHKHATRYTDGKAIPVSRRQ
RLYKITKVSGQKLYLKTLHHWVWARDVTGYWGGSHRSFKLTHKLNLYRNASLTRRTGGYY
VAGDTVHGSLVKAPNGRAYRIKTKLGYLTANVRYSNLA

Enzyme Prediction     

No EC number prediction in MGYG000004860_00576.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	42	206	2.9e-30	0.9717514124293786

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06523	GH25_PlyB-like	2.81e-63	39	218	1	177	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd00599	GH25_muramidase	4.84e-23	40	227	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.
pfam01183	Glyco_hydro_25	1.08e-16	42	207	2	178	Glycosyl hydrolases family 25.
cd06522	GH25_AtlA-like	1.55e-14	42	216	5	189	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.
cd06525	GH25_Lyc-like	2.82e-13	42	214	4	180	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
AYM01837.1	1.53e-172	7	398	6	378
QFR61620.1	8.77e-172	6	398	5	378
SMS13317.1	5.04e-171	6	398	5	378
AKP64857.1	5.81e-170	6	398	4	378
QFR61621.1	4.75e-169	5	398	6	400

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HMC_A	7.27e-19	42	232	9	192	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
4JZ5_A	3.35e-13	40	222	25	216	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
5A6S_A	6.08e-06	40	219	24	202	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000345	0.998880	0.000178	0.000230	0.000170	0.000153

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004860_00576.