CAZyme Information: MGYG000001304_01319

Basic Information

• Species: Erysipelatoclostridium spiroforme
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium spiroforme
• CAZyme ID: MGYG000001304_01319
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
282	MGYG000001304_7|CGC1	33163.31	8.8231

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001304	2507485	Isolate	not provided	North America

• Gene Location: Start: 9320; End: 10168 Strand: -

Full Sequence      

MKYKFFYFLSLSIIIFSCSLYYKQYLPNYLNHSIVMLLVIMFFYLFIFLNKHKRKLTKII
SLVLSICLFFFSFAIFSHNDKLSTDGKYIGIDISKWNKEVNLQLASQEIDYVIIRCGYTS
LSDGKKTKEDPYFKQNLKQCEELSIPYGIYYYSLARDENQAKKEANFVTNLLNNKIPPLG
VFLDLEDEKFQGDLTNNELTTVATTFLENIPNQNKKGIYANHHWWSTKLTDPQLDKYIKW
KARYNDKPTLEEEYAILQYSQTGSIKGIIGNVDLNIVANKYW

Enzyme Prediction     

No EC number prediction in MGYG000001304_01319.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	91	268	1.5e-34	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.97e-66	90	276	3	189	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	6.39e-30	90	277	2	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.
cd06524	GH25_YegX-like	1.26e-19	90	276	2	191	YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.
cd06525	GH25_Lyc-like	4.74e-18	90	275	2	182	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.
cd06523	GH25_PlyB-like	9.45e-17	91	275	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW75611.1	7.37e-132	14	282	24	294
QPS14056.1	7.37e-132	14	282	24	294
QQY27125.1	1.48e-131	14	282	24	294
QQV05922.1	8.54e-131	14	282	24	294
BCL58913.1	5.57e-40	90	275	5	188

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	2.47e-13	91	276	272	466	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	6.03e-13	91	276	272	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
3HMC_A	1.33e-12	86	280	1	183	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.992367	0.000211	0.007413	0.000000	0.000000	0.000008

TMHMM  Annotations     

start	end
5	22
32	49
56	78