CAZyme Information: MGYG000002360_01211

Basic Information

• Species: Lactobacillus hominis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus hominis
• CAZyme ID: MGYG000002360_01211
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
360	MGYG000002360_5|CGC1	39134.07	8.2162

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002360	1926186	Isolate	France	Europe

• Gene Location: Start: 84267; End: 85349 Strand: -

Full Sequence      

MARQFGADVSSNNPPNVNNYARFGSKFVIVKLTEGTTYRNPSAKQQIASAIASGQTPHGY
FFAVFSDNSYLAQLNAELAIYQAKALGLPAGSILATDWEVGDGNEVNGPVSANTQAILVS
MRMIQKAGYKPMLYSGAYNLKNRVNTSLILKEFPDSLWVAAYPLGNGIAVSQPDFSCFPS
MDGVAIWQFTNNWCNQGVDGNIALMDFSKVKNEEVDDELNWHPQVKYNELGQFKINRPNG
ADLYEDASLKKVVGHRPNGATFKINRAKDGAVCAGTNQWFSQADGLTKINPLAVNPYGKG
IAQITADNAWTQNNAKPDAGIKHLEKGSTWHVLGRSGKYLLIGNEQSGKFVDGDKATIVL

Enzyme Prediction     

EC	3.2.1.17

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	8	197	1.1e-33	0.9830508474576272

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06415	GH25_Cpl1-like	1.09e-71	20	204	17	195	Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage.
cd06522	GH25_AtlA-like	6.70e-27	23	202	24	190	AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
pfam01183	Glyco_hydro_25	4.62e-26	24	192	19	174	Glycosyl hydrolases family 25.
smart00641	Glyco_25	1.37e-20	91	208	2	106	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	2.70e-16	24	204	21	183	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIC18527.1	1.72e-119	8	360	9	366
QIH26259.1	1.72e-119	8	360	9	366
QIH25031.1	1.39e-118	8	360	9	366
QIH21231.1	1.13e-117	8	360	9	366
QWS36907.1	1.91e-85	3	360	9	373

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1H09_A	1.98e-23	8	244	9	219	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXU_A	2.00e-23	8	244	10	220	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXV_A	5.18e-23	8	244	10	220	ChainA, LYSOZYME [Streptococcus phage Cp1],2J8F_A Chain A, LYSOZYME [Streptococcus phage Cp1],2J8G_A Chain A, LYSOZYME [Streptococcus phage Cp1]
1OBA_A	3.45e-22	8	244	10	220	ChainA, Lysozyme [Streptococcus phage Cp1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P33486	4.19e-25	1	183	1	181	Lysozyme OS=Lactococcus phage mv1 OX=33769 GN=lysA PE=1 SV=3
P15057	1.10e-22	8	244	10	220	Lysozyme OS=Streptococcus phage Cp-1 OX=10747 GN=CPL1 PE=1 SV=2
P19386	1.51e-22	8	206	10	189	Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 PE=3 SV=1
Q8HA43	9.64e-21	24	290	175	424	D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2
P19385	6.18e-20	24	265	27	242	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2

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
1.000063	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002360_01211.