CAZyme Information: MGYG000000242_03249

Basic Information

• Species: Enterocloster sp000431375
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster sp000431375
• CAZyme ID: MGYG000000242_03249
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
137	MGYG000000242_29|CGC1	15188.1	9.7324

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000242	3795523	Isolate	China	Asia

• Gene Location: Start: 20578; End: 20991 Strand: -

Full Sequence      

MKISDNGLNLIKKFEGCRLTAYQDAVGVWTIGYGTTNADKAITGISIRQGLRISQETADE
WLRQSVDKKYGPKVDKYSAYNWNQNEFDALVSFAYNIGSIDGLTASGSRSKEEIADKIQA
YNKAGGKVLSGLIRRRQ

Enzyme Prediction     

No EC number prediction in MGYG000000242_03249.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	3	137	2.3e-37	0.9781021897810219

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	3.83e-50	7	137	1	129	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.
cd16901	lyz_P1	3.45e-30	3	137	2	133	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	2.94e-25	1	136	5	140	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900	endolysin_R21-like	4.80e-24	10	137	11	135	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	4.74e-09	28	137	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
CBL37136.1	4.77e-54	3	137	4	139
BCK01590.1	1.43e-43	4	137	6	135
AOR64849.1	6.72e-35	1	137	1	138
QIQ67983.1	9.52e-35	1	137	1	138
QAZ64926.1	1.35e-34	1	137	1	138

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	4.59e-25	4	137	53	187	ChainA, Lysozyme [Acinetobacter baumannii]
7M5I_A	1.32e-19	1	137	7	146	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
6H9D_A	4.95e-13	2	98	5	92	ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
2ANV_A	9.19e-13	1	98	2	95	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P62692	1.67e-28	1	137	1	130	Endolysin OS=Lactococcus phage c2 OX=31537 GN=L3 PE=3 SV=1
P62693	1.67e-28	1	137	1	130	Endolysin OS=Lactococcus phage phivML3 OX=10746 GN=L3 PE=3 SV=1
Q37896	1.84e-18	1	137	1	136	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P11187	2.54e-16	1	136	1	135	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P07540	3.54e-16	1	136	1	135	Endolysin OS=Bacillus phage PZA OX=10757 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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000242_03249.