CAZyme Information: MGYG000001512_01662

Basic Information

• Species: Coprobacter secundus
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter secundus
• CAZyme ID: MGYG000001512_01662
• CAZy Family: GH24
• CAZyme Description: Lysozyme RrrD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
144		16294.6	9.9445

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001512	4253015	Isolate	not provided	not provided

• Gene Location: Start: 849841; End: 850275 Strand: +

Full Sequence      

MKTSERGIELIKKFEDFRSEAYKCPAGVWTIGYGHTGGVKPGDRVTETEAEGFLRKDVES
SEKIVLTLVKKPINQNQFDALVSFVYNTGSGNFAGSTLLRKINRNPQDEGIKKEFQKWVY
VKGVKLPGLVSRREKESNLYFSQL

Enzyme Prediction     

No EC number prediction in MGYG000001512_01662.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	4	136	1.4e-50	0.9854014598540146

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	1.60e-72	7	141	1	136	endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd16901	lyz_P1	1.74e-54	3	139	2	138	P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
COG3772	RrrD	1.80e-46	1	140	5	147	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900	endolysin_R21-like	2.64e-45	10	136	11	137	endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
pfam00959	Phage_lysozyme	6.45e-20	28	134	1	107	Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGG11663.1	1.35e-48	1	140	1	139
AZI53711.1	2.98e-45	1	140	1	139
AUS01738.1	3.73e-45	9	140	7	137
QYW02862.1	3.85e-45	1	140	1	137
ANV21598.1	7.29e-45	7	140	7	139

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	2.12e-28	3	143	52	196	ChainA, Lysozyme [Acinetobacter baumannii]
6H9D_A	3.99e-27	2	142	5	148	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
3HDF_A	1.82e-20	22	139	17	134	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
7M5I_A	2.10e-20	1	144	7	157	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
2ANV_A	2.11e-20	1	142	2	146	ChainA, Lysozyme [Lederbergvirus P22],2ANV_B Chain B, Lysozyme [Lederbergvirus P22],2ANX_A Chain A, Lysozyme [Lederbergvirus P22],2ANX_B Chain B, Lysozyme [Lederbergvirus P22]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9T1T5	1.22e-35	1	142	1	145	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
Q37896	4.66e-24	1	142	1	144	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P11187	1.76e-22	1	142	1	144	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P07540	3.45e-22	1	142	1	144	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
O80292	4.36e-21	15	139	37	161	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 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
1.000055	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001512_01662.