Species | Enterocloster sp000431375 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster sp000431375 | |||||||||||
CAZyme ID | MGYG000000242_00131 | |||||||||||
CAZy Family | GH24 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 137356; End: 138123 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH24 | 3 | 139 | 8.9e-37 | 0.9927007299270073 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00737 | lyz_endolysin_autolysin | 6.39e-50 | 7 | 144 | 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. |
cd16901 | lyz_P1 | 1.90e-31 | 3 | 142 | 2 | 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. |
COG3772 | RrrD | 4.80e-30 | 1 | 147 | 5 | 151 | Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis]. |
cd16900 | endolysin_R21-like | 1.54e-25 | 10 | 144 | 11 | 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. |
NF033930 | pneumo_PspA | 3.94e-22 | 146 | 252 | 438 | 530 | pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL37136.1 | 1.10e-58 | 3 | 150 | 4 | 152 |
BCK01590.1 | 3.44e-46 | 4 | 144 | 6 | 142 |
AYH32979.1 | 6.07e-36 | 1 | 145 | 1 | 146 |
AYY08229.1 | 3.50e-35 | 1 | 145 | 2 | 147 |
QIQ67983.1 | 9.56e-35 | 1 | 145 | 1 | 146 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6ET6_A | 1.76e-24 | 4 | 144 | 53 | 194 | ChainA, Lysozyme [Acinetobacter baumannii] |
7M5I_A | 7.00e-19 | 1 | 150 | 7 | 160 | ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15] |
6H9D_A | 2.16e-14 | 2 | 146 | 5 | 149 | ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus] |
2ANV_A | 3.74e-12 | 1 | 145 | 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] |
3HDF_A | 2.92e-06 | 15 | 144 | 10 | 136 | ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P62692 | 2.29e-31 | 1 | 174 | 1 | 175 | Endolysin OS=Lactococcus phage c2 OX=31537 GN=L3 PE=3 SV=1 |
P62693 | 2.29e-31 | 1 | 174 | 1 | 175 | Endolysin OS=Lactococcus phage phivML3 OX=10746 GN=L3 PE=3 SV=1 |
Q37896 | 1.11e-21 | 1 | 145 | 1 | 144 | Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1 |
P11187 | 3.79e-19 | 1 | 167 | 1 | 168 | Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1 |
P07540 | 7.29e-19 | 1 | 167 | 1 | 168 | Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000054 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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