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CAZyme Information: MGYG000004295_02752

You are here: Home > Sequence: MGYG000004295_02752

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Providencia rettgeri
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Providencia; Providencia rettgeri
CAZyme ID MGYG000004295_02752
CAZy Family GH24
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
189 MGYG000004295_76|CGC1 20712.2 9.1728
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004295 4142275 MAG Israel Asia
Gene Location Start: 15212;  End: 15781  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004295_02752.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH24 22 150 1.6e-47 0.9562043795620438

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16900 endolysin_R21-like 3.61e-81 14 155 1 142
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.
cd00737 lyz_endolysin_autolysin 9.41e-59 22 155 2 136
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.
COG3772 RrrD 2.83e-55 22 156 12 149
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901 lyz_P1 1.26e-45 21 155 6 140
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.
pfam00959 Phage_lysozyme 2.04e-30 42 148 1 107
Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QKG44818.1 3.36e-130 1 189 1 189
QNN34951.1 3.36e-130 1 189 1 189
QNP21085.1 1.60e-128 1 189 1 189
BBV04195.1 1.26e-125 1 189 1 189
QIF60556.1 1.25e-123 1 189 1 190

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZPU_A 5.47e-60 6 155 6 161
Thestructure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_B The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_C The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_D The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12]
3HDE_A 4.59e-59 6 155 6 161
ChainA, Lysozyme [Enterobacteria phage P21],3HDE_B Chain B, Lysozyme [Enterobacteria phage P21],3HDE_C Chain C, Lysozyme [Enterobacteria phage P21],3HDE_D Chain D, Lysozyme [Enterobacteria phage P21]
3HDF_A 1.18e-58 29 155 10 136
ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
6ET6_A 2.39e-24 6 155 39 194
ChainA, Lysozyme [Acinetobacter baumannii]
7M5I_A 1.12e-13 25 155 17 154
ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O80292 2.62e-63 10 155 12 163
SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
O80288 2.47e-61 10 155 12 163
SAR-endolysin OS=Bacteriophage PS34 OX=83127 GN=19 PE=3 SV=1
P78285 2.18e-59 6 155 6 161
Lysozyme RrrD OS=Escherichia coli (strain K12) OX=83333 GN=rrrD PE=1 SV=1
P10439 1.25e-58 6 155 6 161
SAR-endolysin OS=Enterobacteria phage PA-2 OX=10738 GN=15 PE=3 SV=1
P27359 2.90e-57 6 155 6 161
SAR-endolysin OS=Enterobacteria phage P21 OX=10711 GN=R PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.979341 0.020420 0.000124 0.000051 0.000025 0.000051

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004295_02752.