A6W7G7
Gene name |
atpA |
Protein name |
ATP synthase subunit alpha |
Names |
ATP synthase F1 sector subunit alpha, F-ATPase subunit alpha |
Species |
Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) |
KEGG Pathway |
kra:Krad_1268 |
EC number |
7.1.2.2: Hydron translocation linked to the hydrolysis of a nucleoside triphosphate |
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 A6W7G7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A6W7G7-F1 | Predicted | AlphaFoldDB |
No variants for A6W7G7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A6W7G7 | |||||
No associated diseases with A6W7G7
5 regional properties for A6W7G7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain | 153 - 376 | IPR000194 |
| domain | ATP synthase, alpha subunit, C-terminal | 383 - 512 | IPR000793 |
| domain | ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain | 30 - 96 | IPR004100 |
| active_site | ATPase, alpha/beta subunit, nucleotide-binding domain, active site | 367 - 376 | IPR020003 |
| domain | ATP synthase, F1 complex, alpha subunit nucleotide-binding domain | 98 - 379 | IPR033732 |
Functions
| Description | ||
|---|---|---|
| EC Number | 7.1.2.2 | Hydron translocation linked to the hydrolysis of a nucleoside triphosphate |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| proton-transporting ATP synthase complex, catalytic core F(1) | The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| proton-transporting ATP synthase activity, rotational mechanism | Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + H2O + phosphate + H+(in) -> ATP + H+(out). |
| proton-transporting ATPase activity, rotational mechanism | Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAELTIRPEE | IRDALDAFVA | SYDPGTAARE | EVGRVTDAGD | GIAHVEGLPS | VMANELLRFQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DGTLGLAQNL | DVRDIGVVVL | GDYAGIEEGQ | EVHRTGEVLS | VPVGDNFLGR | VVDPLGAPID |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GLGPIEAETR | RALELQAPSV | MQRQEVREPL | QTGIKAIDAM | IPVGRGQRQL | IIGDRQTGKS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AIAIDTIINQ | KANWESGDPK | QQVRCIYVAI | GQKGSTIAAV | RRSLEEAGAM | EYTTIVAAPA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SDPAGFKYLA | PYTGSSIGQH | WMYGGKHVLI | VFDDLSKQAE | AYRAVSLLLR | RPPGREAYPG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DVFYLHSRLL | ERCAKLSDEL | GGGSMTGLPF | IETKGNDVSA | YIPTNVISIT | DGQIFLQSDL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FNANQRPAID | VGISVSRVGG | AAQTKAIKGI | SGTLKLDLAQ | FRAMEAFAMF | ASDLDQASRN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QLARGARLVE | LLKQPQYTPF | SLEEQVVSIW | AGTTGQLDSV | EVSDISRFER | EFLEYVKRNH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AGVMQGIRET | KQFSDGAKDE | LKKAVDAFKP | QFSGGSKGSN | VPKDVDAGAT | DADDISQEKI |
| 550 | |||||
| TTRKGGATAA | RG |