CAZyme Information: MGYG000002889_01842

Basic Information

• Species: Pantoea sp002920175
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Pantoea; Pantoea sp002920175
• CAZyme ID: MGYG000002889_01842
• CAZy Family: GH24
• CAZyme Description: Lysozyme RrrD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
160		17262.9	8.7693

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002889	4513078	MAG	United States	North America

• Gene Location: Start: 4152; End: 4634 Strand: -

Full Sequence      

MAAVLGIAALLPSFSTLKISSGGLQLLADAEGCRTSPYQCSAGVWTNGIGHTAGVTPQSV
VSERQVAVNLVDDLIRVERQLSLCVPVAMPQPVWDALVSFAFNVGTGAACRSTMASYLNQ
QRWRAACDQLPRWIYVNGVKSTGLAQRRERERAWCLRGVV

Enzyme Prediction     

No EC number prediction in MGYG000002889_01842.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	19	151	2.9e-43	0.9927007299270073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16901	lyz_P1	1.65e-66	19	156	2	140	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.
cd00737	lyz_endolysin_autolysin	3.35e-45	23	153	1	133	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	7.95e-44	19	159	7	151	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900	endolysin_R21-like	2.81e-40	25	156	10	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	2.22e-15	44	149	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
AUY25605.1	1.98e-78	1	160	10	169
AIX72494.1	1.14e-77	1	160	10	169
AUY26605.1	1.14e-77	1	160	10	169
AYN29707.1	9.37e-77	1	159	10	168
QZQ51993.1	1.33e-76	3	160	12	169

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1XJU_A	4.94e-27	18	160	1	155	ChainA, Lysozyme [Punavirus P1],1XJU_B Chain B, Lysozyme [Punavirus P1]
1XJT_A	4.40e-25	17	160	28	183	ChainA, Lysozyme [Punavirus P1]
3HDF_A	8.34e-20	31	158	10	138	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	1.52e-19	31	158	35	163	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	2.68e-19	31	158	35	163	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
Q37875	3.36e-26	17	160	28	183	SAR-endolysin OS=Escherichia phage P1 OX=2886926 GN=17 PE=1 SV=1
O80292	7.22e-21	31	158	37	165	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
O80288	3.12e-19	31	158	37	165	SAR-endolysin OS=Bacteriophage PS34 OX=83127 GN=19 PE=3 SV=1
Q9T1T5	3.76e-19	17	153	1	141	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P78285	1.17e-18	31	158	35	163	Lysozyme RrrD OS=Escherichia coli (strain K12) OX=83333 GN=rrrD PE=1 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
0.774938	0.224230	0.000296	0.000225	0.000123	0.000199

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002889_01842.