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CAZyme Information: MGYG000004172_01305
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; ; | |||||||||||
| CAZyme ID | MGYG000004172_01305 | |||||||||||
| CAZy Family | GH73 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 355411; End: 356877 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG1705 | FlgJ | 1.04e-29 | 5 | 134 | 59 | 189 | Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility]. |
| NF038016 | sporang_Gsm | 1.05e-29 | 4 | 133 | 175 | 312 | sporangiospore maturation cell wall hydrolase GsmA. The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain. |
| pfam01832 | Glucosaminidase | 4.36e-22 | 1 | 77 | 5 | 77 | Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyze peptidoglycan. |
| smart00047 | LYZ2 | 1.76e-18 | 2 | 133 | 21 | 147 | Lysozyme subfamily 2. Eubacterial enzymes distantly related to eukaryotic lysozymes. |
| cd12797 | M23_peptidase | 6.74e-18 | 192 | 273 | 1 | 85 | M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ADY35004.1 | 0.0 | 1 | 488 | 16 | 503 |
| ABP57346.1 | 5.00e-270 | 1 | 488 | 17 | 516 |
| QCQ41937.1 | 2.88e-269 | 1 | 488 | 17 | 516 |
| QCQ49986.1 | 2.16e-266 | 1 | 488 | 17 | 515 |
| QLK81501.1 | 8.77e-266 | 1 | 488 | 17 | 515 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2ZYC_A | 7.63e-07 | 8 | 145 | 21 | 161 | ChainA, Peptidoglycan hydrolase FlgJ [Sphingomonas sp. A1] |
| 3VWO_A | 1.21e-06 | 8 | 129 | 20 | 148 | Crystalstructure of peptidoglycan hydrolase mutant from Sphingomonas sp. A1 [Sphingomonas sp. A1] |
| 3FI7_A | 3.12e-06 | 1 | 133 | 42 | 183 | CrystalStructure of the autolysin Auto (Lmo1076) from Listeria monocytogenes, catalytic domain [Listeria monocytogenes EGD-e] |
| 3K3T_A | 4.72e-06 | 8 | 145 | 21 | 161 | E185Amutant of peptidoglycan hydrolase from Sphingomonas sp. A1 [Sphingomonas sp. A1] |
| 5T1Q_A | 6.02e-06 | 9 | 133 | 80 | 212 | ChainA, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_B Chain B, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_C Chain C, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_D Chain D, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O32083 | 5.41e-08 | 6 | 133 | 65 | 198 | Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1 |
| P44693 | 1.09e-06 | 141 | 271 | 301 | 431 | Uncharacterized metalloprotease HI_0409 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0409 PE=3 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 |
|---|---|---|---|---|---|
| 1.000024 | 0.000017 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |