CAZyme Information: MGYG000003395_01710

Basic Information

• Species: Superficieibacter sp900766525
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Superficieibacter; Superficieibacter sp900766525
• CAZyme ID: MGYG000003395_01710
• CAZy Family: GH24
• CAZyme Description: Lysozyme RrrD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
145	MGYG000003395_41|CGC5	16177.68	8.2749

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003395	5080781	MAG	United States	North America

• Gene Location: Start: 227855; End: 228292 Strand: -

Full Sequence      

MKISPEGIALIKREEGECLKAYRDTKGILTIGVGHTGLVDGRAITPTLTISKEKSSALLV
ADIAWVEKAINSRVKVPLTQNQYDALCCLVFNIGEPNFAESTVLKRLNNHEYHGAADAFL
MWKRSGNDPDILLPRRQREREVFLT

Enzyme Prediction     

No EC number prediction in MGYG000003395_01710.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	3	139	4.7e-40	0.9927007299270073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	6.50e-59	7	144	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.
COG3772	RrrD	4.35e-38	1	145	5	149	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	2.67e-34	3	141	2	137	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	2.24e-30	8	144	9	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.
pfam00959	Phage_lysozyme	1.69e-24	28	137	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
AST68357.1	2.45e-88	1	145	1	145
APZ06636.1	5.78e-87	1	145	1	145
AZI87171.1	8.21e-87	1	145	1	145
QNQ20733.1	1.93e-85	1	145	1	145
QNQ19401.1	1.93e-85	1	145	1	145

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2ANV_A	1.73e-62	1	145	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]
6ET6_A	1.39e-29	4	144	53	194	ChainA, Lysozyme [Acinetobacter baumannii]
7M5I_A	1.95e-21	1	144	7	154	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
6H9D_A	2.88e-18	2	145	5	148	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
3HDF_A	1.83e-17	15	144	10	136	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P09963	4.71e-62	1	145	2	146	Endolysin OS=Salmonella phage P22 OX=10754 GN=19 PE=1 SV=1
Q9T1T5	1.09e-31	1	143	1	143	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
Q37896	2.94e-21	1	145	1	144	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
O80288	1.54e-18	15	144	37	163	SAR-endolysin OS=Bacteriophage PS34 OX=83127 GN=19 PE=3 SV=1
O80292	2.17e-18	15	144	37	163	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
1.000073	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003395_01710.