CAZyme Information: MGYG000000226_00278

Basic Information

• Species: Lactococcus lactis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Lactococcus; Lactococcus lactis
• CAZyme ID: MGYG000000226_00278
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
271	MGYG000000226_1|CGC6	30935.24	9.743

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000226	2362991	Isolate	China	Asia

• Gene Location: Start: 307126; End: 307941 Strand: -

Full Sequence      

MKPKMRRKLKKMGAFIFTASMIAMIALLGLVRIRPVEPPKKSATEKIVVNHILDEKVLDL
NKPVVDLSGWQRPEDIDYNTLSQHVIGAVIRVNGSYGHADNSASKDGEDTAYKQHIKAFQ
ERGIPTAVYAFVTGENTSEMKKQARDFYRRASPYKPTYYWLDVEVTNMKNMNEGIEAFRS
ELEKQGAKNIGIYAQDWFLRDNQIKVDKFKAIWIAAYGRNTGSWDASPETTLSYKMQQFT
DQGTLPGYSGNVDLNMVNNQTNYNELFKNQK

Enzyme Prediction     

No EC number prediction in MGYG000000226_00278.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	65	247	3.4e-36	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06523	GH25_PlyB-like	2.69e-87	63	257	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.
COG3757	Acm	3.27e-85	5	271	1	267	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06414	GH25_LytC-like	7.23e-26	62	256	1	189	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.
cd00599	GH25_muramidase	3.96e-21	64	257	2	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.
cd06525	GH25_Lyc-like	3.25e-16	65	255	3	182	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
QEA60512.1	2.33e-198	1	271	1	271
QQF01153.1	2.33e-198	1	271	1	271
BAL51040.1	1.92e-197	1	271	1	271
AAK05238.1	4.52e-196	1	271	1	271
QEX48465.1	4.52e-196	1	271	1	271

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4FF5_A	2.79e-69	60	268	50	260	Structurebasis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion [Streptococcus pneumoniae]
3HMC_A	6.98e-21	64	257	7	179	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
2NW0_A	6.77e-18	64	258	3	175	ChainA, PlyB [Bacteriophage sp.],2NW0_B Chain B, PlyB [Bacteriophage sp.]
5A6S_A	2.16e-06	109	260	59	204	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999964	0.000057	0.000001	0.000000	0.000000	0.000005

TMHMM  Annotations     

start	end
12	31