CAZyme Information: MGYG000001352_03715

Basic Information

• Species: Clostridium_AQ sp000165065
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Clostridium_AQ; Clostridium_AQ sp000165065
• CAZyme ID: MGYG000001352_03715
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
450		50727.12	5.0425

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001352	4458401	Isolate	not provided	not provided

• Gene Location: Start: 97850; End: 99202 Strand: -

Full Sequence      

MRKLLVTLLAAGLCLTGVHAQETENTDGTVSTMDANEIKTVTADTYQPVGEMDGAENAAM
GDGTPQQPQPEYRSRSANARLISPVWGMNGTMKTFTYMKDGQSIVVENPKQVVDVSEHDG
KINWEKLKSEGIDAAIIRIGWGVGYTDEYFDYNISECKRLGIPYGLYLYSYAYDANFAYA
EAESTIERLQGYDLTDMSYPIYYDIEAFKEYNHDGATRVPPKDVSTYESIIKTYVDKLNS
AGFSGNVHVYSYRSYCQNQLNSAYILGLTSWIAEYGSYLAFDNQYYTGPNGWQYTSTANF
DGVERENVDVSMFTNSPLNLQTQSPANLTATVEGTNIKLTWDKVPYNTRYRVYYQTTDDG
EWNYLTSQTGTSYTFKTGASGASYRFVVRTANLINGEYKFSQASFSNRLTYPQKKAQGFH
NLSRRVRVFSSPNAANYNRYDPFKKNGWAA

Enzyme Prediction     

No EC number prediction in MGYG000001352_03715.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	113	303	6.8e-35	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.23e-55	110	313	1	190	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.
cd00599	GH25_muramidase	3.77e-25	111	313	1	186	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	9.04e-23	113	303	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	1.29e-20	113	313	3	184	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.
cd06522	GH25_AtlA-like	1.32e-16	110	312	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQR24886.1	2.11e-306	1	445	1	445
ANU71242.1	2.11e-306	1	445	1	445
QIX10955.1	2.11e-306	1	445	1	445
ASU20273.1	2.11e-306	1	445	1	445
QJA04626.1	1.57e-301	1	445	1	445

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	8.49e-45	93	313	252	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	2.27e-44	93	313	252	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A	1.19e-07	111	320	6	209	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRT_A	2.28e-07	113	365	23	269	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]
4KRU_A	2.47e-07	113	303	23	198	X-raystructure of catalytic domain 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	2.89e-09	113	313	12	196	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.27e-06	111	320	83	286	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

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
0.000288	0.998592	0.000553	0.000184	0.000187	0.000159

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001352_03715.