Species | Clostridium beijerinckii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium beijerinckii | |||||||||||
CAZyme ID | MGYG000004667_02222 | |||||||||||
CAZy Family | GH24 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 26012; End: 26866 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH24 | 132 | 268 | 1.2e-31 | 0.9927007299270073 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00737 | lyz_endolysin_autolysin | 5.51e-44 | 136 | 272 | 1 | 135 | 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 | 1.25e-25 | 132 | 272 | 7 | 147 | Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis]. |
COG3409 | PGRP | 8.03e-22 | 4 | 120 | 40 | 184 | Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis]. |
cd16901 | lyz_P1 | 1.33e-19 | 132 | 268 | 2 | 135 | 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. |
pfam01471 | PG_binding_1 | 3.20e-12 | 8 | 64 | 1 | 57 | Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUN37948.1 | 5.28e-181 | 1 | 284 | 1 | 284 |
AQS01884.1 | 1.71e-46 | 1 | 279 | 1 | 289 |
AQS11484.1 | 1.71e-46 | 1 | 279 | 1 | 289 |
AQS15867.1 | 1.71e-46 | 1 | 279 | 1 | 289 |
AQR91982.1 | 1.71e-46 | 1 | 279 | 1 | 289 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7M5I_A | 6.46e-11 | 132 | 279 | 9 | 160 | ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15] |
6ET6_A | 1.19e-10 | 133 | 265 | 53 | 186 | ChainA, Lysozyme [Acinetobacter baumannii] |
6H9D_A | 5.31e-08 | 132 | 234 | 6 | 105 | ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus] |
3BKH_A | 2.70e-07 | 2 | 67 | 11 | 76 | ChainA, lytic transglycosylase [Pseudomonas phage phiKZ],3BKV_A Chain A, lytic transglycosylase [Pseudomonas phage phiKZ] |
2ANV_A | 9.79e-06 | 132 | 265 | 4 | 138 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q37896 | 2.03e-20 | 132 | 283 | 3 | 153 | Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1 |
P07540 | 1.23e-17 | 132 | 275 | 3 | 145 | Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1 |
P11187 | 1.23e-17 | 132 | 275 | 3 | 145 | Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1 |
Q9T1T5 | 1.95e-10 | 132 | 275 | 3 | 146 | Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000057 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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