CAZyme Information: MGYG000002499_00304

Basic Information

• Species: Enterobacter roggenkampii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter roggenkampii
• CAZyme ID: MGYG000002499_00304
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
172		18382.04	8.2944

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002499	4871477	Isolate	Singapore	Asia

• Gene Location: Start: 333715; End: 334233 Strand: -

Full Sequence      

MQNKQKAGAAGAVCSVGAIITLVLGMGNVRTNERGLELIGNAESCRRDPYVCPAGVITDG
IGNTHGVKPGVRKTDEEIAKDWQANILEAEKCVNAYGNGKSLSDNTFSAVTSITFNCGCA
TMRTSTLFKKLQQGEIKQACEQFPRWVYGGGKVLPGLVTRRDAEKQLCLDGI

Enzyme Prediction     

No EC number prediction in MGYG000002499_00304.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	32	164	8.5e-40	0.9854014598540146

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16901	lyz_P1	4.33e-82	30	169	1	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.
COG3772	RrrD	2.06e-49	30	172	6	151	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd00737	lyz_endolysin_autolysin	6.07e-49	35	169	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.
pfam00959	Phage_lysozyme	2.63e-32	58	162	3	107	Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.
cd16900	endolysin_R21-like	1.11e-31	38	169	11	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALQ83103.1	5.11e-99	2	172	3	173
ALQ88598.1	5.11e-99	2	172	3	173
ASV21250.1	5.11e-99	2	172	3	173
QID67285.1	1.46e-98	2	172	3	173
QUL22035.1	1.46e-98	2	172	3	173

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1XJT_A	1.91e-64	1	172	1	182	ChainA, Lysozyme [Punavirus P1]
1XJU_A	8.74e-57	30	172	1	154	ChainA, Lysozyme [Punavirus P1],1XJU_B Chain B, Lysozyme [Punavirus P1]
6ET6_A	5.14e-21	24	169	45	194	ChainA, Lysozyme [Acinetobacter baumannii]
4ZPU_A	8.05e-18	49	171	41	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]
3HDF_A	1.99e-17	49	171	16	138	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
Q37875	1.30e-65	1	172	1	182	SAR-endolysin OS=Escherichia phage P1 OX=2886926 GN=17 PE=1 SV=1
P51728	1.30e-29	30	169	34	184	SAR-endolysin OS=Haemophilus phage HP1 (strain HP1c1) OX=1289570 GN=lys PE=3 SV=1
O80292	1.87e-21	43	171	37	165	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
O80288	8.77e-19	43	171	37	165	SAR-endolysin OS=Bacteriophage PS34 OX=83127 GN=19 PE=3 SV=1
Q9T1T5	2.94e-18	32	167	4	142	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 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
0.877607	0.120788	0.000812	0.000263	0.000168	0.000368

TMHMM  Annotations     

start	end
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