CAZyme Information: MGYG000001304_00060

Basic Information

• Species: Erysipelatoclostridium spiroforme
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium spiroforme
• CAZyme ID: MGYG000001304_00060
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
341	MGYG000001304_1|CGC2	39431.31	5.0182

Genome Property

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

• Gene Location: Start: 77149; End: 78174 Strand: -

Full Sequence      

MLRRDVLTNGIDVSQYQGLINWEVVKNHIDFAIIRCGYGQDIIGQDDELFKRNADECTRL
NIPFGVYLYSYAKNVEDARGEARHVMRLVKDYKMAYPVYYDLEDENTTGRQSNEVIANIA
KAFADELEANGYFVGMYASLYWWKTKLTSEIFDKYTRWVANYAAELNFDKDYDMWQYSST
GWVEGISTIVDLNYCYKDFPKIISEAGKNNFNKNIPVERYKVGDNVRFNYVFLTSESTNP
LRPYRNVGRITKVVKNARNPYLIGEDQGWVNDQVIEGKINYLSNPDYVGDSFVNALKQIG
EDISFENRSRIARLNGINNYVGSATQNLELLQLLKDGRLIS

Enzyme Prediction     

No EC number prediction in MGYG000001304_00060.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	11	186	1.4e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.09e-90	10	196	3	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.
cd00599	GH25_muramidase	1.90e-37	10	194	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.
cd06523	GH25_PlyB-like	3.56e-25	11	194	3	176	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.
cd06524	GH25_YegX-like	1.88e-22	10	194	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.
COG3757	Acm	6.70e-22	10	194	65	252	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW73604.1	6.89e-202	8	341	3	336
QPS13132.1	6.89e-202	8	341	3	336
QQV05001.1	6.89e-202	8	341	3	336
QQY28033.1	2.80e-201	8	341	3	336
BCL58913.1	1.68e-167	6	339	1	333

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	4.21e-26	11	196	272	468	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	1.07e-25	11	196	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4FF5_A	5.28e-11	11	193	55	247	Structurebasis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion [Streptococcus pneumoniae]
3HMC_A	6.85e-11	11	193	8	177	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
2NW0_A	1.91e-09	11	193	4	172	ChainA, PlyB [Bacteriophage sp.],2NW0_B Chain B, PlyB [Bacteriophage sp.]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	1.13e-08	10	193	3	178	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999847	0.000174	0.000007	0.000001	0.000000	0.000002

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001304_00060.