CAZyme Information: MGYG000000019_02571

Basic Information

• Species: Enterobacter cloacae_O
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter cloacae_O
• CAZyme ID: MGYG000000019_02571
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
112		12565.47	4.7906

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000019	4947669	Isolate	United Kingdom	Europe

• Gene Location: Start: 32621; End: 32959 Strand: -

Full Sequence      

MTGYALQISSAAIALIKKQQGLSLEKYRDENGLWVIGYGHVIRQWEKFNGPITPAEAEYL
LLDDIQLCETLLRETIGRPLPQQQHDALVLTLFSFGNESLVPETILQAVARV

Enzyme Prediction     

No EC number prediction in MGYG000000019_02571.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	8	109	3.5e-23	0.7518248175182481

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	2.44e-26	12	109	1	98	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	1.28e-16	7	107	6	107	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	2.66e-09	7	106	1	99	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	4.59e-07	13	65	3	57	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	4.69e-07	8	95	4	86	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
QLA68753.1	1.95e-76	1	112	1	112
QKZ97310.1	3.11e-73	1	112	1	112
QPO59847.1	6.03e-62	1	112	1	112
QPP01735.1	6.03e-62	1	112	1	112
AJB72835.1	6.03e-62	1	112	1	112

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4EVX_A	1.35e-18	7	98	6	96	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]
2ANV_A	5.08e-11	6	107	2	106	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]
7M5I_A	1.01e-08	6	107	7	110	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
Q9T1T5	1.67e-12	6	107	1	100	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P09963	1.41e-10	6	107	2	106	Endolysin OS=Salmonella phage P22 OX=10754 GN=19 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
1.000047	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000019_02571.