CAZyme Information: MGYG000003675_02020

Basic Information

• Species: Faecalibacterium sp900551435
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium sp900551435
• CAZyme ID: MGYG000003675_02020
• CAZy Family: GH25
• CAZyme Description: Autolytic lysozyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
210		23280.84	8.7678

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003675	2696714	MAG	Peru	South America

• Gene Location: Start: 21743; End: 22375 Strand: +

Full Sequence      

MPDTIMDVSRWQGTIDWKKVKASGKVNGVMLRTVATNTAYGGIYIDPTFEKNYWGCVEAG
LPVGAYCYTKAVTADYAAKELVKLKVALEGKSFQLPVAVDAEDPALLSLSPEALAQIIKM
EAKQIEKWGLYAMVYTYTSFADTALAMNELTDFDLWIADYRSKRPSRKHGMWQYTNKGVV
SGVNGVVDLSHAYKDYPKIIQKAGLTGKWG

Enzyme Prediction     

No EC number prediction in MGYG000003675_02020.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	183	1.5e-39	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.69e-43	6	177	4	175	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	2.71e-24	7	175	4	169	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	1.65e-23	7	177	2	174	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	2.55e-22	6	177	3	169	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.
cd06524	GH25_YegX-like	1.65e-18	7	177	4	177	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATL89415.1	2.32e-87	5	210	4	207
ATO99829.1	6.66e-82	4	205	3	202
QIA41786.1	6.66e-82	4	205	3	202
ATL90045.1	1.55e-80	4	205	3	202
ATL89796.1	1.72e-62	1	206	1	212

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	8.50e-14	5	201	24	210	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2WAG_A	1.15e-10	6	193	19	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
2WW5_A	5.69e-10	5	193	271	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]
1JFX_A	3.64e-09	6	188	8	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	2.33e-18	6	190	70	252	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	2.33e-18	6	190	70	252	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	4.49e-18	6	190	70	252	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P34020	2.70e-15	6	189	4	177	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
P26836	3.09e-15	6	190	12	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

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
1.000087	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003675_02020.