CAZyme Information: MGYG000001008_02565

Basic Information

• Species: Clostridium_AQ sp900552125
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Clostridium_AQ; Clostridium_AQ sp900552125
• CAZyme ID: MGYG000001008_02565
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
467		51784	4.5781

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001008	3113530	MAG	Austria	Europe

• Gene Location: Start: 18940; End: 20343 Strand: -

Full Sequence      

MKFYKGLSAFLLVAGIILLPLNNNDNLKAENNVANGFEGVEIVTEDTYQPIDPDVSEELE
NVAMGSSIEQPKARMARASAPYWDESSGVKKFYDAEGNLMYHEGTKKVIDVSEHNGKIDW
DKVKASGVDGAIIRVGWGYLGEDKYFQRNVSECNRLGIPYGVYLYSYAYDANFAYAEANG
TAEMLSKVNLNLSYPIYYDIERFDDWNDNGTTRVPPKNAAEYEKVIGTYISRMEQLGYAG
KVHVYSYRSYLQNQLNSPKILPYVSWIAAYTPTLGFNNTYYNGEEGWQYTSTGSVGGVSG
RVDISCFSNQFYNLSLSTSVPDEILNVFTSVGARFEGGYVRGLPLNTDLTTLSNSLSAIG
NITCFNKAGNIVSGGIIGTGQRISITPTQNNEEMKTYTVMIVVKGDVDGDGQIRSIDYSL
VKNDILNLKKLNDGYLIAGDIDGDGRIRSIDYSLIKNDILNLKKIEQ

Enzyme Prediction     

EC	3.2.1.17

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	109	298	4.9e-37	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	4.39e-71	106	307	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	1.10e-36	107	303	1	182	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.
cd06523	GH25_PlyB-like	4.54e-23	107	305	1	175	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
pfam01183	Glyco_hydro_25	4.50e-20	109	298	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	5.38e-20	107	307	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBK23561.1	6.86e-177	11	437	14	460
BBK63284.1	6.86e-177	11	437	14	460
BCT44110.1	1.20e-96	37	404	39	394
QQR24886.1	1.14e-92	5	324	2	328
ANU71242.1	1.14e-92	5	324	2	328

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	2.65e-58	83	305	246	465	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	7.23e-58	83	305	246	465	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
5A6S_A	1.84e-07	106	311	22	205	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2WAG_A	2.35e-07	107	307	17	206	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	5.48e-08	107	337	10	227	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	8.76e-06	107	308	2	181	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.013894	0.749092	0.236035	0.000342	0.000297	0.000314

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001008_02565.