O66605
Gene name |
lon |
Protein name |
Lon protease |
Names |
ATP-dependent protease La |
Species |
Aquifex aeolicus (strain VF5) |
KEGG Pathway |
aae:aq_242 |
EC number |
3.4.21.53: Serine endopeptidases |
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 O66605
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O66605-F1 | Predicted | AlphaFoldDB |
No variants for O66605
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O66605 | |||||
No associated diseases with O66605
5 regional properties for O66605
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Lon protease, N-terminal domain | 16 - 212 | IPR003111 |
| domain | AAA+ ATPase domain | 362 - 510 | IPR003593 |
| domain | ATPase, AAA-type, core | 367 - 504 | IPR003959 |
| active_site | Peptidase S16, active site | 689 - 697 | IPR008268 |
| domain | Peptidase S16, Lon proteolytic domain | 584 - 787 | IPR008269 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.21.53 | Serine endopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
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. |
5 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. |
| sequence-specific DNA binding | Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. |
| serine-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). |
2 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNELFQTPQV | EAGIKEYPLM | PLRDIVIFPT | MVQPLFVGRR | FSIRAIEEAN | KKDKLIFLVL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QKDKDVEEPK | EEDIYKVGVV | AYILRTVPIE | DARVKVLVQG | LKRGVIKKLE | WKEDHYVAQV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DVIEERDIPP | ESQTIEDKAL | IKAVKESIDK | LVSLGKQIIP | DLVVLIKELE | EPGKLADMVA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SILDIKSSQA | QEILETFDPR | ERLKKVYKFL | QDEIGLLEVK | QRISEIARER | MEKEQREYYL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RQQLKAIQEE | LGEAGGIKAE | IEEYTKKFEE | VKECMPEEGV | KEVEKNIKRL | ERLHPESAEA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GVIRTWLDWV | LDLPWCTRTE | DNYDLERARE | ILDRDHYDLE | KVKDRIIEYL | AIRKLTQGKE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| APTQILAFVG | PPGVGKTSLG | RSIAEALGRK | FVRIALGGIR | DEAEIRGHRR | TYVGAMPGRI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IQAIKQAGTK | NPVIMLDEID | KLAISFQGDP | AAALLEVLDP | EQNKKFTDLY | IGIPFDLSEV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IFICTGNRAD | TIPTPLLDRM | ELIMLSGYSE | EEKLFIAKKH | LIPKLIPLHG | FSPEEIEFTD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EAILEIIRGY | TREAGVRNLQ | RQISAVLRKI | AVKKLQGEKG | PFNITPELVR | KLLGVPRYRP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EREKKPLVGV | ATGLAWTEVG | GEIMFIEATK | MKGKGSLVLT | GSLGDIMKES | AQAALSYIRS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KAEDYGIDPD | IFSQVDVHVH | VPEGAVPKDG | PSAGVAIATA | LLSLFTDIPV | RMDVAMTGEI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| TLRGRVLPVG | GLKEKILAAK | RAEIYEVILP | AKNKDEVMEE | LPEYVREKMT | LHFVDNLEEV |
| 790 | |||||
| FKIALVREPK | PLKEA |