CAZyme Information: MGYG000001499_00488

Basic Information

• Species: Muricomes contortus_B
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Muricomes; Muricomes contortus_B
• CAZyme ID: MGYG000001499_00488
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
322	MGYG000001499_5|CGC2	35531.51	4.4022

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001499	5155658	Isolate	not provided	not provided

• Gene Location: Start: 125112; End: 126080 Strand: +

Full Sequence      

MSTRGLDVSEFQGTVDWEQVKAAGYQFAMLRAGYGFGTLDQQFQRNAAECNRIGLPIGVY
WFCYAISPETARQEADGCINAISSYRLDYPICYDIEQATVNYAAQNGVTLTPALATQFVR
SFCDRIEERGYYAMFYSNRNFLNTYFPADLSDRYALWYAYYNSQFDGTNCGIWQFTDQGS
VPGISGNVDLDTGFIDYPAVIRKAGLNHLDGGSNPAPPPVQDYITYVVQPGDTLSGIAAR
YGTTYQTLAALNGITNPNLIYAGQTIRIPEDGSSTARYYTIQPGDTLSGIAQKFGTTVSE
LQRLNGISNPNLIYAGNTIRIS

Enzyme Prediction     

No EC number prediction in MGYG000001499_00488.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	7	184	7.7e-46	0.9887005649717514
CBM50	226	269	2.6e-17	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.00e-84	4	191	2	188	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	2.99e-40	4	191	1	184	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.
cd06525	GH25_Lyc-like	3.52e-28	4	191	1	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.
cd06413	GH25_muramidase_1	9.86e-28	3	190	3	186	Uncharacterized bacterial muramidase containing 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	2.41e-24	6	190	3	174	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
QYX27151.1	3.28e-141	1	321	1	325
QHB23957.1	1.02e-140	1	270	1	267
QEI31463.1	1.02e-140	1	270	1	267
QRT30197.1	1.02e-140	1	270	1	267
QEK16471.1	9.67e-136	1	321	1	325

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.16e-15	6	190	272	464	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	2.81e-15	6	190	272	464	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRU_A	1.89e-10	4	191	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
5JCD_A	2.97e-10	226	321	85	191	Crystalstructure of OsCEBiP [Oryza sativa Japonica Group],5JCD_B Crystal structure of OsCEBiP [Oryza sativa Japonica Group],5JCD_C Crystal structure of OsCEBiP [Oryza sativa Japonica Group]
4KRT_A	4.70e-10	4	191	21	205	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q49UX4	3.99e-20	225	322	87	194	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
Q6GJK9	4.88e-18	226	322	93	202	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=sle1 PE=3 SV=1
Q37896	2.38e-17	225	321	164	262	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
Q6GC24	8.03e-17	226	322	93	202	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=sle1 PE=3 SV=1
Q2FJH7	8.03e-17	226	322	93	202	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain USA300) OX=367830 GN=sle1 PE=3 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
1.000051	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001499_00488.