Species | Salmonella enterica | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Salmonella; Salmonella enterica | |||||||||||
CAZyme ID | MGYG000002366_00280 | |||||||||||
CAZy Family | GH24 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 306351; End: 306707 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH24 | 9 | 104 | 3.6e-20 | 0.7518248175182481 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3772 | RrrD | 1.05e-39 | 1 | 118 | 1 | 124 | Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis]. |
cd00737 | lyz_endolysin_autolysin | 9.43e-19 | 12 | 107 | 1 | 102 | 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. |
cd00735 | T4-like_lys | 1.32e-06 | 17 | 64 | 7 | 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 | 7.91e-06 | 13 | 108 | 9 | 109 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGR38179.1 | 5.88e-83 | 1 | 118 | 1 | 118 |
QBM54589.1 | 5.88e-83 | 1 | 118 | 1 | 118 |
QQI30595.1 | 8.36e-83 | 1 | 118 | 1 | 118 |
AIK94580.1 | 8.36e-83 | 1 | 118 | 1 | 118 |
AKW00788.2 | 8.36e-83 | 1 | 118 | 1 | 118 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4EVX_A | 1.77e-67 | 5 | 107 | 4 | 106 | 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] |
6H9D_A | 5.66e-06 | 7 | 110 | 5 | 112 | ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9T1T5 | 4.69e-10 | 13 | 109 | 8 | 108 | 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 |
---|---|---|---|---|---|
1.000051 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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