CAZyme Information: MGYG000002472_01710

Basic Information

• Species: Lentilactobacillus kefiri
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lentilactobacillus; Lentilactobacillus kefiri
• CAZyme ID: MGYG000002472_01710
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
299	MGYG000002472_1|CGC20	33428.73	10.4822

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002472	2568073	Isolate	Italy	Europe

• Gene Location: Start: 1733427; End: 1734326 Strand: -

Full Sequence      

MKFRKIAGLLMGAVAAFTFAINASAAKTKIADVSQYQGNINWSKASKQLKFAIIRVQHGD
TGDADFRIDTHKNINANGAYKYNVPFGQYGYAEFSSVADAKKEARDFYKRASSKARFYVL
DNEHRKGHGSEQSYVNAWLAQMRKLTNKPLVYYSYQNYVNVHKINYSKFDGSWIANYSAK
PNVTTDLWQYTSHGSLSGISGRVDLSKAVKGSVVNSWLKTSSKDAAKPTYFTSLPSDKKI
STSKNVYQYKDVNFKSRVSKITAGKKLSVKSITRSNGGAYRFQLSNGNYITANKAYVTD

Enzyme Prediction     

No EC number prediction in MGYG000002472_01710.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	32	199	3.2e-32	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06523	GH25_PlyB-like	7.92e-63	29	207	1	176	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	3.41e-27	29	208	1	186	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	4.30e-24	29	206	2	188	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.
pfam19087	DUF5776	5.74e-19	230	297	1	67	Domain of unknown function (DUF5776). Presumed stalk domain found in bacterial surface proteins forming tandem repeats with high sequence identity. This domain is also associated with other known bacterial surface protein stalks and adhesive domains.
pfam01183	Glyco_hydro_25	2.05e-18	32	199	2	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGV24978.1	2.01e-213	1	299	1	299
AFS01195.1	1.21e-194	1	299	3	301
QUX04736.1	4.93e-194	1	299	3	301
AEB74362.1	4.93e-194	1	299	3	301
QOJ84029.1	3.32e-192	2	299	4	301

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HMC_A	8.32e-22	30	221	7	191	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
2NW0_A	7.85e-20	30	207	3	173	ChainA, PlyB [Bacteriophage sp.],2NW0_B Chain B, PlyB [Bacteriophage sp.]
5A6S_A	1.07e-07	29	206	23	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
4KRU_A	1.37e-06	32	207	24	206	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	1.66e-06	32	207	9	201	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.48e-09	32	286	13	262	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 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
0.000380	0.998731	0.000220	0.000225	0.000221	0.000186

TMHMM  Annotations     

start	end
7	26