Species | Prevotella salivae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella salivae | |||||||||||
CAZyme ID | MGYG000001360_00200 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 212326; End: 213249 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1705 | FlgJ | 1.18e-33 | 30 | 174 | 44 | 193 | Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility]. |
NF038016 | sporang_Gsm | 3.64e-33 | 30 | 169 | 161 | 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. |
smart00047 | LYZ2 | 5.03e-26 | 22 | 165 | 1 | 141 | Lysozyme subfamily 2. Eubacterial enzymes distantly related to eukaryotic lysozymes. |
pfam01832 | Glucosaminidase | 6.67e-25 | 37 | 165 | 1 | 91 | 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. |
PRK12711 | flgJ | 6.55e-17 | 55 | 156 | 241 | 351 | flagellar assembly peptidoglycan hydrolase FlgJ. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
VEH15664.1 | 7.81e-192 | 2 | 307 | 1 | 306 |
BCS86660.1 | 7.90e-153 | 21 | 307 | 2 | 288 |
ALO49150.1 | 1.24e-146 | 2 | 307 | 1 | 305 |
AGB29226.1 | 1.96e-146 | 21 | 307 | 22 | 308 |
ADE83099.1 | 3.94e-133 | 11 | 306 | 9 | 302 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VWO_A | 8.82e-12 | 30 | 160 | 2 | 143 | Crystalstructure of peptidoglycan hydrolase mutant from Sphingomonas sp. A1 [Sphingomonas sp. A1] |
2ZYC_A | 1.05e-11 | 30 | 160 | 3 | 144 | ChainA, Peptidoglycan hydrolase FlgJ [Sphingomonas sp. A1] |
3K3T_A | 6.91e-11 | 30 | 160 | 3 | 144 | E185Amutant of peptidoglycan hydrolase from Sphingomonas sp. A1 [Sphingomonas sp. A1] |
5T1Q_A | 1.94e-06 | 48 | 185 | 79 | 230 | 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] |
3FI7_A | 7.39e-06 | 30 | 169 | 31 | 183 | CrystalStructure of the autolysin Auto (Lmo1076) from Listeria monocytogenes, catalytic domain [Listeria monocytogenes EGD-e] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9X9J3 | 6.09e-12 | 30 | 159 | 161 | 301 | Peptidoglycan hydrolase FlgJ OS=Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) OX=223926 GN=flgJ PE=3 SV=1 |
O32083 | 1.65e-11 | 30 | 169 | 49 | 198 | Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1 |
Q9KQ15 | 7.46e-06 | 31 | 159 | 163 | 302 | Peptidoglycan hydrolase FlgJ OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=flgJ PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000227 | 0.999151 | 0.000164 | 0.000155 | 0.000146 | 0.000135 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.