CAZyme Information: MGYG000001487_00115

Basic Information

• Species: Beduini massiliensis
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Beduini; Beduini massiliensis
• CAZyme ID: MGYG000001487_00115
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
410		45712.54	3.9771

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001487	2850586	Isolate	not provided	not provided

• Gene Location: Start: 105362; End: 106594 Strand: -

Full Sequence      

MSQLGIDISEFQGALNFEAIAGNIDYVIIRAGYADVVDPQFERSYAECKRLNIPCGTYYY
SYALNTEEALAEADFYLSLLEGKAFEYPIYLDMEDGDHYKEEHGLTDPQAYVDITQTFLS
RVESQNNYVGIYSSQAWFDKCLDAPSLKRYDRWIANWGTNDGTIQVDVSDRAGMLQYTSV
GSIEGYDGNVDRDIAYLDYPSIIVGGHFNGNGQNIEPPAQTEYKIGDHVVFESCYRSSTA
KIGWPPEGEALVPDINHGVITAIYDGTNNPYLINDGMCFVNNGDIQGYYEVKQTTYEVGD
HVMFNSCYRSSTAAIGWPPFGEALVPDVDHGVITAIYKGTNNPYLINDGMCFVNNGDITG
YYDKNTYVVQAGDTLSEIAEQYGISYQALAQMNQISDPNLIYPGQILRVP

Enzyme Prediction     

No EC number prediction in MGYG000001487_00115.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	185	1.7e-37	0.9887005649717514
CBM50	367	410	1e-16	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.79e-60	5	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	8.65e-34	5	195	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	1.80e-24	4	194	1	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.
pfam01183	Glyco_hydro_25	7.10e-21	6	185	1	179	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	2.14e-20	5	193	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW75290.1	2.84e-56	1	287	1	273
QQY26763.1	2.84e-56	1	287	1	273
QPS14372.1	2.84e-56	1	287	1	273
QQV06256.1	1.11e-55	1	287	1	273
BCT44624.1	5.33e-54	1	350	1	344

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	3.93e-14	6	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	9.32e-14	6	196	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4JZ5_A	5.08e-10	1	205	21	222	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
5JIP_A	1.80e-08	1	287	12	326	Crystalstructure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens],5JIP_B Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens]
2L9Y_A	1.96e-06	342	410	40	108	Solutionstructure of the MoCVNH-LysM module from the rice blast fungus Magnaporthe oryzae protein (MGG_03307) [Pyricularia oryzae 70-15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9CH26	9.85e-06	363	410	401	448	Teichoic acids export ATP-binding protein TagH OS=Lactococcus lactis subsp. lactis (strain IL1403) OX=272623 GN=tagH 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
1.000056	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001487_00115.