CAZyme Information: MGYG000000330_02031

Basic Information

• Species: Lentilactobacillus parabuchneri
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lentilactobacillus; Lentilactobacillus parabuchneri
• CAZyme ID: MGYG000000330_02031
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
301	MGYG000000330_13|CGC1	33688.89	10.2746

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000330	2487416	MAG	Sweden	Europe

• Gene Location: Start: 41965; End: 42870 Strand: -

Full Sequence      

MTFKFKKIAGLLMGAMAAFTISVNASAAKTKIADVSQYQGSINWSKASKQLKFAIIRVQH
GDTGDADFRIDTQKDINANGAYKYNVPFGQYGYAEFSSVADAKKEARDFYKRSSSKARFY
VLDNEHRKGKGSEQSYVNAWLSQMRKLTKKPLVYYSYQNYVNVHKINYSKFDGSWIANYS
AQPNVTTDLWQYTSKGRLSGISGNVDLSKVVDSSTVNSWLKTTSADVAKPTYFTSLPSDK
QVTTSKNIYEYQDVNFKSRVSKITAGKSLSVKSITRSNGGAYRFQLTNGNYITANKAYVT
D

Enzyme Prediction     

No EC number prediction in MGYG000000330_02031.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	34	201	1.7e-32	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06523	GH25_PlyB-like	2.73e-62	31	210	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	1.78e-28	31	210	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	1.84e-26	31	208	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.
COG3757	Acm	1.17e-18	31	221	64	264	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
pfam19087	DUF5776	1.19e-18	232	299	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOJ84029.1	8.20e-214	1	301	1	301
QOP50037.1	8.20e-214	1	301	1	301
APR07473.1	8.20e-214	1	301	1	301
AFS01195.1	2.59e-201	1	301	1	301
QUX04736.1	1.05e-200	1	301	1	301

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HMC_A	4.45e-22	32	219	7	187	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
2NW0_A	2.18e-20	32	210	3	174	ChainA, PlyB [Bacteriophage sp.],2NW0_B Chain B, PlyB [Bacteriophage sp.]
4JZ5_A	1.06e-16	32	208	25	210	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
4FF5_A	5.14e-11	32	210	54	249	Structurebasis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion [Streptococcus pneumoniae]
5A6S_A	2.49e-08	31	212	23	203	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	8.36e-10	34	288	13	262	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.44e-06	34	209	86	278	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

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
0.000436	0.998790	0.000203	0.000204	0.000185	0.000162

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000330_02031.