CAZyme Information: MGYG000002498_00571

Basic Information

• Species: Enterobacter sichuanensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter sichuanensis
• CAZyme ID: MGYG000002498_00571
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
427	MGYG000002498_1|CGC6	45629.53	7.6954

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002498	4685711	Isolate	Singapore	Asia

• Gene Location: Start: 592630; End: 593913 Strand: +

Full Sequence      

MAYSLTWLPDVLEAAGLKVAECTGWRTRGRGDVGTIRGVICHHTAGAPQGVMPSLNTLIN
GRAASANAKALAGPLAQLGLARDGTLFIVAAGRANHAGVGSWQSIDTGNTNFIGIEAENT
GIGEPWPDVQLDAYYRAVAAILKYIGAPETMVCGHKEYALPKGRKNDPTLDMAVFRNQVG
QIMRGTAQVRPAIPAMDASGRATLRRGTKGELVKQIQFTIGIYDDGIFGSNTEAAVRVFQ
RNHALVPDGIVGPKTWYELTRLETLSTGQQATTAPSDMGKYTPNQACVDLIKHFESCELE
AYPDPGSGGEPWTIGWGSTGPDINKGTQWTQAECDARFESDLMNYGSKVAALLGNAPTSG
NQFGALTSFAYNAGLHALAESTLLRKHKAGNFEGAAEEFGRWIYGSGKLLPGLVRRRTAE
AQLYRTS

Enzyme Prediction     

No EC number prediction in MGYG000002498_00571.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	285	420	1.4e-41	0.9781021897810219

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	6.26e-56	287	425	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.
cd16900	endolysin_R21-like	5.49e-35	290	423	11	140	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	3.99e-34	285	427	9	150	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	1.46e-28	284	423	3	138	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	1.54e-18	312	417	2	106	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
QFQ11460.1	9.32e-105	278	427	1	150
QBX83332.1	6.74e-81	288	426	1	139
QEA14912.1	1.83e-51	288	425	55	197
AQR76009.1	2.38e-51	282	424	2	151
ATY33999.1	2.83e-49	282	424	2	151

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	3.35e-21	279	424	49	193	ChainA, Lysozyme [Acinetobacter baumannii]
7M5I_A	1.09e-15	288	424	14	153	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
3HDF_A	1.72e-15	312	423	24	134	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	3.10e-15	312	423	49	159	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	7.18e-15	312	423	49	159	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
Q37896	7.71e-18	284	426	4	144	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
Q9T1T5	2.54e-16	290	427	10	146	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P07540	4.48e-15	284	424	4	142	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
P62692	1.22e-14	284	424	4	136	Endolysin OS=Lactococcus phage c2 OX=31537 GN=L3 PE=3 SV=1
P62693	1.22e-14	284	424	4	136	Endolysin OS=Lactococcus phage phivML3 OX=10746 GN=L3 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
1.000046	0.000010	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002498_00571.