Overview
Basic information about this protein and its source genome.
- Accession
- PA5558
- Gene
- PA5558 atpF
- Status
- annotated
- Amino acids
- 156
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- Localization
- CytoplasmicMembrane
Selected Druggability evidence
Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
6- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
- GO:0045259 A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient.
- GO:0046933 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 + phosphate + 5 H+(out) => ATP + H2O + 4 H+(in).
- GO:0015986 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a membrane to generate an electrochemical gradient (proton-motive force).
- GO:0015078 Enables the transfer of a proton from one side of a membrane to the other.
- GO:0045263 OBSOLETE. All non-F1 subunits of a hydrogen-transporting ATP synthase, including integral and peripheral membrane proteins.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 6 | 137 | CDD | cd06503 | ATP-synt_Fo_b |
| 63 | 121 | SUPERFAMILY | SSF81573 | F1F0 ATP synthase subunit B, membrane domain |
| 63 | 121 | InterPro | IPR028987 | F-type ATP synthase subunit B-like, membrane domain superfamily |
| 6 | 136 | Pfam | PF00430 | ATP synthase B/B' CF(0) |
| 6 | 136 | InterPro | IPR002146 | ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast |
| 7 | 29 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 62 | 121 | Gene3D | G3DSA:1.20.5.620 | F1F0 ATP synthase subunit B, membrane domain |
| 2 | 155 | PANTHER | PTHR33445 | ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC |
| 34 | 156 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 62 | 122 | FunFam | G3DSA:1.20.5.620:FF:000001 | ATP synthase subunit b |
| 44 | 122 | Coils | Coil | Coil |
| 12 | 33 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 10 | 155 | NCBIfam | TIGR01144 | F0F1 ATP synthase subunit B |
| 10 | 155 | InterPro | IPR005864 | ATP synthase, F0 complex, subunit b, bacterial |
| 1 | 138 | Hamap | MF_01398 | ATP synthase subunit b [atpF]. |
| 1 | 138 | InterPro | IPR002146 | ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast |
| 1 | 11 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA5558
|
AlphaFold | — | — | full sequence | — | Viewing |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 1 | 0.754 |