P0ABH9
Gene name |
clpA (lopD, b0882, JW0866) |
Protein name |
ATP-dependent Clp protease ATP-binding subunit ClpA |
Names |
|
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b0882 |
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
28 structures for P0ABH9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1K6K | X-ray | 180 A | A | 1-143 | PDB |
| 1KSF | X-ray | 260 A | X | 1-758 | PDB |
| 1LZW | X-ray | 250 A | B | 1-146 | PDB |
| 1MBU | X-ray | 230 A | A/B | 1-142 | PDB |
| 1MBV | X-ray | 330 A | A | 1-142 | PDB |
| 1MBX | X-ray | 225 A | A/B | 1-142 | PDB |
| 1MG9 | X-ray | 230 A | B | 1-146 | PDB |
| 1R6B | X-ray | 225 A | X | 1-758 | PDB |
| 1R6C | X-ray | 215 A | X | 1-143 | PDB |
| 1R6O | X-ray | 225 A | A/B | 1-143 | PDB |
| 1R6Q | X-ray | 235 A | A/B | 1-143 | PDB |
| 5OFO | EM | 460 A | A/B/C/D/E/F | 609-635 | PDB |
| 5OG1 | EM | 450 A | A/B/C/D/E/F | 609-635 | PDB |
| 6UQE | EM | 300 A | A/B/C/D/E/F | 169-746 | PDB |
| 6UQO | EM | 310 A | A/B/C/D/E/F | 169-746 | PDB |
| 6W1Z | EM | 270 A | A/B/C/D/E/F | 1-758 | PDB |
| 6W20 | EM | 300 A | A/B/C/D/E/F | 1-758 | PDB |
| 6W21 | EM | 330 A | A/B/C/D/E/F | 1-758 | PDB |
| 6W22 | EM | 300 A | A/B/C/D/E/F | 1-758 | PDB |
| 6W23 | EM | 310 A | A/B/C/D/E/F | 1-758 | PDB |
| 6W24 | EM | 340 A | A/B/C/D/E/F | 1-758 | PDB |
| 7UIV | EM | 338 A | A/B/C/D/E/F | 1-758 | PDB |
| 7UIW | EM | 333 A | A/B/C/D/E/F | 1-758 | PDB |
| 7UIX | EM | 324 A | A/B/C/D/E/F | 1-758 | PDB |
| 7UIY | EM | 322 A | A/B/C/D/E/F | 1-758 | PDB |
| 7UIZ | EM | 324 A | A/B/C/D/E/F | 1-758 | PDB |
| 7UJ0 | EM | 326 A | A/B/C/D/E/F | 1-758 | PDB |
| AF-P0ABH9-F1 | Predicted | AlphaFoldDB |
No variants for P0ABH9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0ABH9 | |||||
No associated diseases with P0ABH9
9 regional properties for P0ABH9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | AAA+ ATPase domain | 206 - 352 | IPR003593-1 |
| domain | AAA+ ATPase domain | 487 - 654 | IPR003593-2 |
| domain | ATPase, AAA-type, core | 211 - 342 | IPR003959-1 |
| domain | ATPase, AAA-type, core | 486 - 647 | IPR003959-2 |
| domain | Clp, repeat (R) domain | 1 - 145 | IPR004176 |
| conserved_site | ClpA/B, conserved site 1 | 302 - 314 | IPR018368 |
| domain | Clp ATPase, C-terminal | 653 - 744 | IPR019489 |
| conserved_site | ClpA/B, conserved site 2 | 518 - 536 | IPR028299 |
| domain | ClpA/ClpB, AAA lid domain | 350 - 452 | IPR041546 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endopeptidase Clp complex | A protein complex comprised of members of the ClpX, ClpC, ClpD, ClpP or ClpR protein families. ClpPs are the proteolytic subunit of active complexes, and ClpA and ClpX form the regulatory subunits. Enzymatically active and inactive complexes can form. |
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. |
| ATP-dependent peptidase activity | Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to heat | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
| protein quality control for misfolded or incompletely synthesized proteins | The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins. |
| protein unfolding | The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state. |
| response to oxidative stress | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLNQELELSL | NMAFARAREH | RHEFMTVEHL | LLALLSNPSA | REALEACSVD | LVALRQELEA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FIEQTTPVLP | ASEEERDTQP | TLSFQRVLQR | AVFHVQSSGR | NEVTGANVLV | AIFSEQESQA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AYLLRKHEVS | RLDVVNFISH | GTRKDEPTQS | SDPGSQPNSE | EQAGGEERME | NFTTNLNQLA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RVGGIDPLIG | REKELERAIQ | VLCRRRKNNP | LLVGESGVGK | TAIAEGLAWR | IVQGDVPEVM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ADCTIYSLDI | GSLLAGTKYR | GDFEKRFKAL | LKQLEQDTNS | ILFIDEIHTI | IGAGAASGGQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VDAANLIKPL | LSSGKIRVIG | STTYQEFSNI | FEKDRALARR | FQKIDITEPS | IEETVQIING |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LKPKYEAHHD | VRYTAKAVRA | AVELAVKYIN | DRHLPDKAID | VIDEAGARAR | LMPVSKRKKT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VNVADIESVV | ARIARIPEKS | VSQSDRDTLK | NLGDRLKMLV | FGQDKAIEAL | TEAIKMARAG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LGHEHKPVGS | FLFAGPTGVG | KTEVTVQLSK | ALGIELLRFD | MSEYMERHTV | SRLIGAPPGY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VGFDQGGLLT | DAVIKHPHAV | LLLDEIEKAH | PDVFNILLQV | MDNGTLTDNN | GRKADFRNVV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LVMTTNAGVR | ETERKSIGLI | HQDNSTDAME | EIKKIFTPEF | RNRLDNIIWF | DHLSTDVIHQ |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VVDKFIVELQ | VQLDQKGVSL | EVSQEARNWL | AEKGYDRAMG | ARPMARVIQD | NLKKPLANEL |
| 730 | 740 | 750 | |||
| LFGSLVDGGQ | VTVALDKEKN | ELTYGFQSAQ | KHKAEAAH |