P22068
Gene name |
atp2 (SPAC222.12c) |
Protein name |
ATP synthase subunit beta, mitochondrial |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAC222.12c |
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 P22068
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P22068-F1 | Predicted | AlphaFoldDB |
2 variants for P22068
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_970338_C_T | 8 | S>N | No | Jeffares_SNPs | |
| I_969863_A_T | 166 | D>E | No | Jeffares_SNPs |
No associated diseases with P22068
4 regional properties for P22068
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain | 183 - 401 | IPR000194 |
| domain | AAA+ ATPase domain | 195 - 378 | IPR003593 |
| domain | ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain | 57 - 126 | IPR004100 |
| active_site | ATPase, alpha/beta subunit, nucleotide-binding domain, active site | 392 - 401 | IPR020003 |
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 | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial proton-transporting ATP synthase complex | A proton-transporting ATP synthase complex found in the mitochondrial membrane. |
| mitochondrial proton-transporting ATP synthase, catalytic core | The hexamer, comprising three alpha and three beta subunits, that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ADP binding | Binding to ADP, adenosine 5'-diphosphate. |
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proton motive force-driven mitochondrial ATP synthesis | The transport of protons across a mitochondrial membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLKKQALSGI | RRFSLATKQS | FVKTSYKLPR | KSWLNTAKFN | TIRYASTEAA | KHNKGSIKQV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IGAVVDCQFE | DADSLPSILN | ALEVKLPDNK | RLVLEVAQHV | GENTVRTIAM | DGTEGLVRGT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AVIDTGSPIS | IPVGPGTLGR | IMNVIGEPVD | ERGPIKAVKY | SPIHADAPSF | EEQSTTPEIL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ETGIKVVDLL | APYARGGKIG | LFGGAGVGKT | VFIQELINNI | AKAHGGYSVF | TGVGERTREG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NDLYREMQET | GVIKLEGESK | AALVFGQMNE | PPGARARVAL | TGLTVAEYFR | DIEGQDVLLF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IDNIFRFTQA | GSEVSALLGR | IPSAVGYQPT | LATDMGAMQE | RITTTKKGSI | TSVQAVYVPA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DDLTDPAPAT | TFAHLDATTV | LSRSISELGI | YPAVDPLDSK | SRMMDPRILG | EEHYNLAGSV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QQMLQEYKSL | QDIIAILGMD | ELSEADKLTV | ERARKVQRFL | SQPFAVAEVF | TGIEGRLVSL |
| 490 | 500 | 510 | 520 | ||
| KDTIRSFKEI | LEGKHDSLPE | SAFYMVGSID | DAVKKAEKIA | QELAA |