CAZyme Information: MGYG000001294_02432

Basic Information

• Species: Parasutterella excrementihominis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Parasutterella; Parasutterella excrementihominis
• CAZyme ID: MGYG000001294_02432
• CAZy Family: GH24
• CAZyme Description: Lysozyme RrrD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
154		17240.78	6.2451

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001294	2614765	Isolate	not provided	not provided

• Gene Location: Start: 2326; End: 2790 Strand: +

Full Sequence      

MTQDILLYPPELATQFISEFEQGPKGGPALESYKCPAGVWTIGFGHTKDVHAGEHITRNE
AYDLLTKDLVQTQEELAAIVKVPVTENQFIALMSWLFNLGLTPAVRRSTLLRKLNAGDYE
GAAEEFPKWRKSAGQVLPGLVNRRAEEKKIFLKE

Enzyme Prediction     

No EC number prediction in MGYG000001294_02432.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	14	147	7.2e-44	0.9562043795620438

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	4.95e-60	15	152	3	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.
cd16900	endolysin_R21-like	1.01e-45	13	152	8	142	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	9.36e-44	10	153	8	149	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	2.57e-41	33	148	21	136	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.
pfam00959	Phage_lysozyme	8.44e-19	39	145	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
SQI43374.1	1.52e-39	17	153	11	141
QYW02862.1	1.06e-37	15	152	7	138
QXF34290.1	1.42e-37	27	152	16	140
CAQ85210.1	1.63e-36	27	152	16	140
CAQ85669.1	1.63e-36	27	152	16	140

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	7.33e-26	27	154	65	196	ChainA, Lysozyme [Acinetobacter baumannii]
3HDF_A	7.06e-23	23	152	2	136	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	1.33e-22	23	152	27	161	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	3.36e-22	23	152	27	161	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]
6H9D_A	4.37e-20	15	152	12	147	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9T1T5	3.71e-32	27	151	16	143	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
Q37896	6.92e-23	40	152	31	143	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P11187	4.79e-22	27	151	16	142	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P27359	7.27e-22	23	152	27	161	SAR-endolysin OS=Enterobacteria phage P21 OX=10711 GN=R PE=1 SV=1
P07540	9.39e-22	27	151	16	142	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 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
1.000067	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001294_02432.