CAZyme Information: MGYG000002542_00982

Basic Information

• Species: Lentilactobacillus parafarraginis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lentilactobacillus; Lentilactobacillus parafarraginis
• CAZyme ID: MGYG000002542_00982
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
254	MGYG000002542_47|CGC2	29672.95	10.2948

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002542	2852137	Isolate	not provided	not provided

• Gene Location: Start: 70193; End: 70957 Strand: +

Full Sequence      

MRRKDVQPIYAETYRRRVRTRRVVFGIFLVILALVAAFSIWRWHAQQELKKYPIKGVMID
QSNGYIDFESLKSDGVKFVYLKATQGAAFTDDNFQSNFQRSQGSQLPIGVYHYFSFTSSA
TAQFKNFVRQVTTNTGGLPICVAVQYYGTFDASSLHWPLVRKRLRQLMDELHRYYQRPVM
ISASRDIISRLKIAATHKHQFWVTDGQLGKPNADDTFIQVTDKQSFKVDRQILFLPMTVF
NGNEKQWDRYLDEN

Enzyme Prediction     

No EC number prediction in MGYG000002542_00982.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	59	225	3.4e-30	0.96045197740113

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06419	GH25_muramidase_2	9.56e-55	47	240	1	190	Uncharacterized bacterial muramidase containing 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.
cd06413	GH25_muramidase_1	1.01e-31	52	242	1	191	Uncharacterized bacterial muramidase containing 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.
cd00599	GH25_muramidase	4.19e-30	55	223	1	171	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	1.52e-19	55	217	1	158	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.
COG3757	Acm	8.96e-17	48	203	57	213	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEU39092.1	5.79e-140	1	251	1	251
QIR09946.1	5.79e-140	1	251	1	251
QHB52582.1	1.17e-139	1	252	1	252
AEB73903.1	2.19e-130	1	252	1	252
AFS00729.1	2.19e-130	1	252	1	252

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	2.85e-25	49	250	11	216	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	9.66e-11	54	128	20	94	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.20e-10	54	128	20	94	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]
1JFX_A	1.65e-08	54	188	5	136	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2X8R_A	5.09e-06	54	186	4	141	Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8FFY2	1.43e-11	52	252	65	266	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	1.96e-11	52	252	65	266	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
P26836	1.41e-10	54	128	9	83	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.62e-08	54	132	1	78	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P25310	1.57e-07	54	188	82	213	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

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
0.999672	0.000200	0.000015	0.000001	0.000001	0.000134

TMHMM  Annotations     

start	end
23	45