CAZyme Information: MGYG000002386_02325

Basic Information

• Species: Lactiplantibacillus plantarum
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactiplantibacillus; Lactiplantibacillus plantarum
• CAZyme ID: MGYG000002386_02325
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
258	MGYG000002386_1|CGC34	28982.93	10.0573

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002386	3412302	Isolate	China	Asia

• Gene Location: Start: 2391477; End: 2392253 Strand: -

Full Sequence      

MTKRQHYRPVYAKTRWARWRYRLGWLLVLLIIIGSVWGGLAWLRWRSDAVVSGFDVRGVA
VSQNDGYLDFAALQNDGLKFVYLHATQGASYTDDNFASNYERIVGTSLGVGVIHTFSFSS
TAAAQAAYFEKTVGDSIGNLPIAIQVQYYGDYTDQTIAVRKSRAKLKALVTTLNQDYNRS
CVVWSTPAVAKQIVKPALKDTDLWLDTAKTHQQGQRVMFMHYSDRAVYRQNGTRQEFAGI
LFNGSVTAYNKVVAQGLN

Enzyme Prediction     

No EC number prediction in MGYG000002386_02325.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	60	225	5.1e-27	0.9548022598870056

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06419	GH25_muramidase_2	3.78e-92	49	242	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.
cd00599	GH25_muramidase	2.51e-40	57	227	1	173	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.
cd06413	GH25_muramidase_1	7.28e-25	56	225	3	174	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.
cd06525	GH25_Lyc-like	1.60e-14	57	205	1	144	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.
cd06412	GH25_CH-type	2.29e-11	56	134	1	80	CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYA97478.1	3.43e-189	1	258	1	258
AYG34197.1	3.43e-189	1	258	1	258
AOB21461.1	3.43e-189	1	258	1	258
QDX83932.1	3.43e-189	1	258	1	258
ATL78321.1	3.43e-189	1	258	1	258

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.91e-19	54	210	14	170	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	8.92e-08	55	205	19	167	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.59e-07	55	205	19	167	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.44e-07	55	205	8	156	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.46e-06	56	246	1	190	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

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
1.000037	0.000020	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
21	43