CAZyme Information: MGYG000000021_01291

Basic Information

• Species: Limosilactobacillus vaginalis_A
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus vaginalis_A
• CAZyme ID: MGYG000000021_01291
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
305	MGYG000000021_14|CGC1	34297.85	4.9515

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000021	1945993	Isolate	United Kingdom	Europe

• Gene Location: Start: 7253; End: 8170 Strand: -

Full Sequence      

MALYFTDVFSGSADWIVTDPHAQGTIVKASQGTGYVNPKYEYQYSLAKTNGRLLGLYHYA
GGNDPVAEATYFLDHIRGKVGEAVLAVDWEQYQNAAWGNPNWVRKFVDEVHRQTNVWPLI
YVQESAIWQVANCANDCGLWVAKYPSMNWHSWQVPDMQVNTAPWPGYTLWQFAGDDEDRS
IATVDRNGWQRLANPTGQVSSRPLIFGDSSASSISNNETWTDNLGDTWHREVGRFTSSRP
LTLRWGALPTSTAIAELPAGSVIDYDAWSRHDGEVWIRQPRGNGQYGYLPCRNAVTNEAY
GTFSE

Enzyme Prediction     

No EC number prediction in MGYG000000021_01291.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	14	174	7.9e-32	0.8983050847457628

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	3.01e-60	7	189	5	195	LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
cd00599	GH25_muramidase	7.72e-35	4	187	1	184	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.
pfam01183	Glyco_hydro_25	2.58e-23	23	172	21	171	Glycosyl hydrolases family 25.
cd06412	GH25_CH-type	8.16e-19	7	175	5	182	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.
cd06525	GH25_Lyc-like	2.70e-16	26	172	26	166	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
QWS03256.1	4.62e-182	1	303	1	296
QDR72396.1	2.19e-180	1	303	1	296
QKT15282.1	7.30e-179	1	303	1	296
AGR65183.1	7.68e-179	1	303	12	307
AGN99135.1	5.50e-173	1	303	1	292

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZM8_A	7.69e-12	27	172	29	181	ChainA, muramidase [Sodiomyces alcalophilus]
6AKV_A	5.47e-09	230	303	205	281	ChainA, LysB4 [Bacillus phage B4]
2X8R_A	1.96e-07	22	179	26	196	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
P00721	1.33e-09	22	171	24	184	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 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
1.000057	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000021_01291.