CAZyme Information: MGYG000002503_01498

Basic Information

• Species: Enterobacter ludwigii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter ludwigii
• CAZyme ID: MGYG000002503_01498
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
169		18363.41	9.4178

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002503	4697885	Isolate	Australia	Oceania

• Gene Location: Start: 211311; End: 211820 Strand: +

Full Sequence      

MNSIIKRCSAAGVLALAVLMPDFRLLNTSPEGLALIADLEGCRLSPYRCSAGVWTSGIGH
TSGVVPGREITEREAAANLVADVMNVERRLAVCAPVEMPPRVYDALVSFAFNVGTGAACR
STLVSFIKRKQWPQACNQLTRWVYVNGVKNAGLENRRAREKAWCLKGMP

Enzyme Prediction     

No EC number prediction in MGYG000002503_01498.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	29	160	1.4e-44	0.9854014598540146

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16901	lyz_P1	3.59e-71	28	165	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	2.34e-50	32	162	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	3.37e-49	28	169	7	152	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900	endolysin_R21-like	9.81e-41	11	165	1	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	2.10e-15	53	158	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
QDE51715.1	5.13e-122	1	169	1	169
AVO99701.1	5.13e-122	1	169	1	169
QLW28061.1	5.13e-122	1	169	1	169
QCV81540.1	5.13e-122	1	169	1	169
AHE69161.1	5.13e-122	1	169	1	169

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1XJU_A	3.31e-27	27	168	1	154	ChainA, Lysozyme [Punavirus P1],1XJU_B Chain B, Lysozyme [Punavirus P1]
1XJT_A	2.95e-25	27	168	29	182	ChainA, Lysozyme [Punavirus P1]
6ET6_A	4.60e-16	27	166	51	195	ChainA, Lysozyme [Acinetobacter baumannii]
6H9D_A	8.89e-11	29	165	7	147	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
7M5I_A	5.68e-09	26	160	7	149	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q37875	3.19e-26	27	168	29	182	SAR-endolysin OS=Escherichia phage P1 OX=2886926 GN=17 PE=1 SV=1
P51728	6.82e-22	8	165	11	184	SAR-endolysin OS=Haemophilus phage HP1 (strain HP1c1) OX=1289570 GN=lys PE=3 SV=1
Q6XQ98	1.51e-21	35	166	22	160	SAR-endolysin OS=Escherichia phage T1 OX=1921008 GN=12 PE=3 SV=1
Q9T1T5	4.89e-19	26	162	1	141	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
Q37896	6.96e-15	26	167	1	145	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 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
0.580087	0.407705	0.010880	0.000540	0.000275	0.000499

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002503_01498.