CAZyme Information: MGYG000001536_01313

Basic Information

• Species: Enterobacter_A timonensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter_A; Enterobacter_A timonensis
• CAZyme ID: MGYG000001536_01313
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
154		17351.84	6.3231

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001536	4199690	Isolate	not provided	not provided

• Gene Location: Start: 34508; End: 34972 Strand: -

Full Sequence      

MFHHRLRISSDGIALIKKFQGLSLEKYCDESGLWVIGYGHVITPSDNFSKLITPLHAEYL
LYQDLRECEDNLSEIVDFRLTQNQHDALISLLFSSGRSRLVQTGIIREIKRGCYANAMQI
WQNETAINGTSVASLTALRQAECALFFTGLAIEA

Enzyme Prediction     

No EC number prediction in MGYG000001536_01313.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	8	142	6.7e-26	0.9927007299270073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	4.21e-35	12	147	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	9.97e-22	4	150	3	151	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	9.04e-10	7	145	1	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.
cd00735	T4-like_lys	8.52e-08	13	117	3	115	bacteriophage T4-like lysozymes. Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.
cd16900	endolysin_R21-like	2.26e-05	13	145	9	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMR75708.1	1.88e-49	1	146	1	146
AEN66903.1	4.36e-48	1	146	1	146
QDE52116.1	3.20e-35	4	111	4	111
QCV81941.1	3.20e-35	4	111	4	111
AWC84388.1	1.84e-34	4	111	4	111

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4EVX_A	2.58e-18	7	104	6	105	Crystalstructure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],4EVX_B Crystal structure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
6H9D_A	4.14e-17	5	148	3	148	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
2ANV_A	8.35e-16	6	148	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	4.46e-15	9	146	53	193	ChainA, Lysozyme [Acinetobacter baumannii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9T1T5	1.12e-19	6	146	1	143	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P09963	2.31e-15	6	148	2	146	Endolysin OS=Salmonella phage P22 OX=10754 GN=19 PE=1 SV=1
Q37896	5.68e-11	6	149	1	145	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P07540	1.97e-10	6	149	1	145	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
P11187	2.72e-10	6	149	1	145	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001536_01313.