CAZyme Information: MGYG000000196_02161

Basic Information

• Species: Bacteroides thetaiotaomicron
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides thetaiotaomicron
• CAZyme ID: MGYG000000196_02161
• CAZy Family: GH24
• CAZyme Description: Lysozyme RrrD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
144		16041.56	10.0069

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000196	6397474	Isolate	China	Asia

• Gene Location: Start: 238976; End: 239410 Strand: -

Full Sequence      

MRTTTGTKNKIKQFEGLRLKAYVCAAGVCTIGYGHTTGVKPGDVITEARADAFFESDIRA
VENQVNALPLHLGQYQFDAVVSFCFNVGIGKFKKSTLYKKIRADAYEPSIPAEFKKWIYG
GGKILPGLVTRREWEAKRYQGLTI

Enzyme Prediction     

No EC number prediction in MGYG000000196_02161.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	9	135	1.2e-44	0.948905109489051

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	4.41e-65	11	140	5	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	5.63e-48	11	135	10	135	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.
cd16900	endolysin_R21-like	1.03e-37	11	135	12	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.
COG3772	RrrD	3.32e-37	11	137	15	145	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
pfam00959	Phage_lysozyme	1.07e-15	30	133	3	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
QDM07514.1	1.55e-104	1	144	1	144
QUU09268.1	1.55e-104	1	144	1	144
QDH56032.1	1.55e-104	1	144	1	144
QQA06365.1	1.55e-104	1	144	1	144
QUT29423.1	2.38e-99	1	144	1	144

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	5.03e-23	11	135	60	189	ChainA, Lysozyme [Acinetobacter baumannii]
6H9D_A	2.19e-17	11	132	14	139	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
3HDF_A	5.46e-16	15	135	10	131	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	9.42e-16	15	135	35	156	ChainA, Lysozyme [Enterobacteria phage P21],3HDE_B Chain B, Lysozyme [Enterobacteria phage P21],3HDE_C Chain C, Lysozyme [Enterobacteria phage P21],3HDE_D Chain D, Lysozyme [Enterobacteria phage P21]
4ZPU_A	1.62e-15	15	135	35	156	Thestructure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_B The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_C The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_D The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9T1T5	1.94e-29	11	140	11	144	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P11187	2.31e-23	9	135	9	138	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P07540	4.54e-23	9	135	9	138	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
Q37896	4.97e-23	9	135	9	138	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
O80292	9.60e-20	15	135	37	158	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
0.829886	0.031337	0.137936	0.000139	0.000225	0.000476

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000196_02161.