CAZyme Information: MGYG000001696_01532

Basic Information

• Species: Enterococcus_A raffinosus
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_A; Enterococcus_A raffinosus
• CAZyme ID: MGYG000001696_01532
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
457		50554.88	7.6017

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001696	4207346	Isolate	India	Asia

• Gene Location: Start: 46859; End: 48232 Strand: +

Full Sequence      

MKRKILGLCFLSVLCLNFSTIALAEENQIESSQQITQSSSTTDSTASVSQIESQTTGNFD
SEQTSDSVETEEVTVPQSQMETAEGTMSLPKGRSDLYPSIQLFASLPSVSATNTNTPSKS
FIDISSHNGNISVANFQKMKGYGVTGVVVKLTEATSYTNPYAQSQINNAMAAGMKVSAYH
YSWFTSDAQAVAEANYFAAAAKKFGLSSGTVMVNDIEEPQILGKGNHTNNSRAFESRLKS
LGYGNVRHYIGLNWLDTGRINAATIGYKNIWVAAYPYNLSTTNFYTQYGAWQWSSQLSFP
GISGNFDINADYTSTFSNPTPTPPANSVQMYRVYNPNSGEHFYTQNVAEKNNLVSKGWRY
EGIGWNGPTSGNPVYRLYNPNAGDHHYTLHAYEKDNLIKKGWRYEGISWYSGGPNALHRL
YNPNAKSGAHHYTLNTNEKNNLVKHGWKYEGLAWYAK

Enzyme Prediction     

No EC number prediction in MGYG000001696_01532.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	122	302	1.9e-39	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06522	GH25_AtlA-like	1.02e-71	119	312	1	192	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	2.31e-38	122	302	1	180	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	6.70e-28	121	310	2	185	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.
cd06414	GH25_LytC-like	2.66e-26	122	312	4	191	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.
cd06415	GH25_Cpl1-like	2.60e-17	121	308	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QXJ58081.1	4.45e-265	1	427	1	429
QZO07829.1	7.35e-264	1	427	1	429
QCQ13646.1	1.93e-220	1	427	1	423
AYQ23282.1	1.93e-220	1	427	1	423
AXG38334.1	5.70e-217	1	427	1	431

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	7.45e-08	119	309	22	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1H09_A	8.99e-06	121	284	7	161	ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXU_A	9.02e-06	121	284	8	162	ChainA, LYSOZYME [Streptococcus phage Cp1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19385	5.12e-06	121	284	8	162	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000430	0.998719	0.000327	0.000180	0.000171	0.000149

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001696_01532.