P0ABI1
Gene name |
clpA (Z1119, ECs0968) |
Protein name |
ATP-dependent Clp protease ATP-binding subunit ClpA |
Names |
|
Species |
Escherichia coli O157:H7 |
KEGG Pathway |
ecs:ECs_0968 |
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 P0ABI1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0ABI1-F1 | Predicted | AlphaFoldDB |
No variants for P0ABI1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0ABI1 | |||||
No associated diseases with P0ABI1
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 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 |