Q03V27
Gene name |
atpA |
Protein name |
ATP synthase subunit alpha |
Names |
ATP synthase F1 sector subunit alpha, F-ATPase subunit alpha |
Species |
Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y) |
KEGG Pathway |
lme:LEUM_1871 |
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 Q03V27
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q03V27-F1 | Predicted | AlphaFoldDB |
No variants for Q03V27
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q03V27 | |||||
No associated diseases with Q03V27
6 regional properties for Q03V27
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | 124 - 575 | IPR004364 |
| domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | 18 - 102 | IPR004365 |
| domain | Aminoacyl-tRNA synthetase, class II | 144 - 572 | IPR006195 |
| domain | GAD domain | 314 - 414 | IPR029351 |
| domain | Aspartate-tRNA ligase, type 1, anticodon recognition domain | 2 - 140 | IPR047089 |
| domain | Aspartate-tRNA ligase, type 1, core domain | 144 - 576 | IPR047090 |
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 |
| MAIQAEEISA | LIKQQLEKFD | TTLTVEEVGT | VTYVGDGVAR | ATGLANALAG | ELVEFANGTY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GMAQNLESSE | VGIIILGGFD | DIREGDTVKR | TGRIMEVPVG | EQLIGRVVNA | LGQPIDGLGE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IKTDKTRPVE | VKAPGVMERK | SVSEPLQTGI | KAIDALVPIG | RGQRELIIGD | RKTGKTSLAI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DTILNQKDQN | MIVIYVAIGQ | KNSTVRAQVE | TLRQMGAMDY | TIVVNAGPSE | PAPMLYLAPY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VGAAMGEEFM | YNGKHVLIVY | DDLSKQATAY | RELSLILRRP | PGREAYPGDV | FYLHSRLLER |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AAKLSDELGG | GSMTALPFIE | TQAGDVSAYI | PTNVISITDG | QVFLDADQFY | AGVRPAIDAG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TSVSRVGGDA | QIKAMKKVAG | TLRLDLASFR | ELESFAQFGS | DLDSATQAKL | ARGRRTVEIL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KQPLNKPMPV | QHQVVVLYAL | THGYLDDVEV | ADIQRFQDEL | IAYVDANASE | LFKAIVETKN |
| 490 | 500 | ||||
| LPEEADLNAA | IEAFKAGFAG | SESAE |