| Species | Pseudomonas_E extremaustralis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E extremaustralis | |||||||||||
| CAZyme ID | MGYG000003208_04432 | |||||||||||
| CAZy Family | GH73 | |||||||||||
| CAZyme Description | Peptidoglycan hydrolase FlgJ | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 26033; End: 26956 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH73 | 157 | 291 | 1.4e-34 | 0.9453125 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK05684 | flgJ | 2.80e-112 | 1 | 291 | 4 | 297 | flagellar assembly peptidoglycan hydrolase FlgJ. |
| TIGR02541 | flagell_FlgJ | 1.76e-101 | 7 | 291 | 1 | 293 | flagellar rod assembly protein/muramidase FlgJ. The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring. |
| PRK12712 | flgJ | 1.65e-83 | 7 | 291 | 16 | 342 | flagellar rod assembly protein/muramidase FlgJ; Provisional |
| PRK12713 | flgJ | 5.30e-73 | 24 | 307 | 34 | 339 | flagellar rod assembly protein/muramidase FlgJ; Provisional |
| PRK12709 | flgJ | 8.38e-72 | 7 | 292 | 14 | 320 | flagellar rod assembly protein/muramidase FlgJ; Provisional |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| SDG37352.1 | 3.35e-216 | 1 | 307 | 1 | 307 |
| AQY68337.1 | 1.53e-199 | 3 | 307 | 6 | 310 |
| AUG09820.1 | 7.51e-189 | 1 | 307 | 1 | 302 |
| AUO44678.1 | 1.11e-162 | 3 | 305 | 6 | 320 |
| AEV60802.1 | 1.11e-162 | 3 | 305 | 6 | 320 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5DN5_A | 5.91e-42 | 149 | 288 | 6 | 145 | Structureof a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],5DN5_B Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],5DN5_C Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2] |
| 5DN4_A | 9.25e-42 | 149 | 288 | 6 | 145 | Structureof the glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2] |
| 3VWO_A | 1.17e-34 | 147 | 288 | 2 | 143 | Crystalstructure of peptidoglycan hydrolase mutant from Sphingomonas sp. A1 [Sphingomonas sp. A1] |
| 2ZYC_A | 1.52e-34 | 147 | 288 | 3 | 144 | ChainA, Peptidoglycan hydrolase FlgJ [Sphingomonas sp. A1] |
| 3K3T_A | 1.17e-33 | 147 | 288 | 3 | 144 | E185Amutant of peptidoglycan hydrolase from Sphingomonas sp. A1 [Sphingomonas sp. A1] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P75942 | 3.00e-67 | 8 | 288 | 12 | 291 | Peptidoglycan hydrolase FlgJ OS=Escherichia coli (strain K12) OX=83333 GN=flgJ PE=3 SV=1 |
| P58231 | 8.45e-67 | 8 | 288 | 12 | 291 | Peptidoglycan hydrolase FlgJ OS=Escherichia coli O157:H7 OX=83334 GN=flgJ PE=3 SV=1 |
| P15931 | 7.34e-66 | 8 | 288 | 12 | 294 | Peptidoglycan hydrolase FlgJ OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=flgJ PE=1 SV=1 |
| Q9KQ15 | 4.64e-44 | 6 | 291 | 9 | 306 | Peptidoglycan hydrolase FlgJ OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=flgJ PE=3 SV=2 |
| Q9X9J3 | 7.96e-42 | 6 | 291 | 9 | 305 | Peptidoglycan hydrolase FlgJ OS=Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) OX=223926 GN=flgJ PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000062 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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