P22608
Gene name |
pilB (PA4526) |
Protein name |
Type IV pilus assembly ATPase PilB |
Names |
|
Species |
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
KEGG Pathway |
pae:PA4526 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P22608
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P22608-F1 | Predicted | AlphaFoldDB |
11 variants for P22608
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 26 | V>L | strain: PAK [UniProt] | No | ||
| 30 | A>T | strain: PAK [UniProt] | No | ||
| 46 | S>N | strain: PAK [UniProt] | No | ||
| 74 | K>R | strain: PAK [UniProt] | No | ||
| 109 | P>A | strain: PAK [UniProt] | No | ||
| 146 | S>N | strain: PAK [UniProt] | No | ||
| 164 | I>VGVKETSG | strain: PAK [UniProt] | No | ||
| 175 | A>TG | strain: PAK [UniProt] | No | ||
| 467 | E>D | strain: PAK [UniProt] | No | ||
| 470 | R>K | strain: PAK [UniProt] | No | ||
| 481 | D>EL | strain: PAK [UniProt] | No |
No associated diseases with P22608
4 regional properties for P22608
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cryptochrome/DNA photolyase, FAD-binding domain | 241 - 395 | IPR005101 |
| domain | DNA photolyase, N-terminal | 2 - 153 | IPR006050 |
| conserved_site | Cryptochrome/DNA photolyase class 1, conserved site, C-terminal | 290 - 302 | IPR018394-1 |
| conserved_site | Cryptochrome/DNA photolyase class 1, conserved site, C-terminal | 310 - 329 | IPR018394-2 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| metal ion binding | Binding to a metal ion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cell motility | Any process involved in the controlled self-propelled movement of a cell that results in translocation of the cell from one place to another. |
| protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| type IV pilus assembly | The assembly from its constituent parts of a type IV pilus. |
| type IV pilus-dependent motility | Any process involved in the controlled movement of a bacterial cell which is dependent on the presence of type IV pili. Includes social gliding motility and twitching motility. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNDSIQLSGL | SRQLVQANLL | DEKTAVQAQA | QAQRNKLSLV | THLVQSKLVS | GLALAELSAE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QFGIAYCDLN | SLDKESFPRD | AISEKLVRQH | RVIPLWRRGN | KLFVGISDPA | NHQAINDVQF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| STGLTTEAIL | VEDDKLGLAI | DKLFESATDG | LAGLDDVDLE | GLDIGSADKS | TQEDASAEAD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DAPVVRFVNK | MLLDAIKGGS | SDLHFEPYEK | IYRVRFRTDG | MLHEVAKPPI | QLASRISARL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KVMAGLDISE | RRKPQDGRIK | MRVSKTKSID | FRVNTLPTLW | GEKIVMRILD | SSSAQMGIDA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LGYEEDQKEL | YLAALKQPQG | MILVTGPTGS | GKTVSLYTGL | NILNTTDINI | STAEDPVEIN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LEGINQVNVN | PRQGMDFSQA | LRAFLRQDPD | VIMVGEIRDL | ETAEIAIKAA | QTGHMVMSTL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HTNSAAETLT | RLLNMGVPAF | NLATSVNLII | AQRLARKLCS | HCKKEHEVPR | ETLLHEGFPE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DKIGTFKLYS | PVGCDHCKNG | YKGRVGIYEV | VKNTPALQRI | IMEEGNSIEI | AEQARKEGFN |
| 550 | 560 | ||||
| DLRTSGLLKA | MQGITSLEEV | NRVTKD |