Protein profile

PA5559

ATP synthase subunit C

Genome: NC_002516.2

Gene: atpE PA5559 Structure source: AlphaFold UniProt Q9HT15
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Amino acids 85
Annotations 9
Features 27
PDB binders 4
Druggability 0.95

Overview

Basic information about this protein and its source genome.

Accession
PA5559
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
atpE PA5559
Status
annotated
Amino acids
85
Structure source
AlphaFold
GO
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:0033177 A protein complex that forms part of a proton-transporting two-sector ATPase complex and carries out proton transport across a membrane. The proton-transporting domain (F0, V0, or A0) includes integral and peripheral membrane proteins. GO:0008289 Binding to a lipid. 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).

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.

FPocket 0.95
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Gene Ontology (GO)

9
  • 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:0033177 A protein complex that forms part of a proton-transporting two-sector ATPase complex and carries out proton transport across a membrane. The proton-transporting domain (F0, V0, or A0) includes integral and peripheral membrane proteins.
  • GO:0008289 Binding to a lipid.
  • 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:1902600 The directed movement of a proton across a membrane.
  • 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.

27 records
Show feature table
Start End DB Term Name
2 77 Gene3D G3DSA:1.20.20.10 F1F0 ATP synthase subunit C
2 77 InterPro IPR038662 F1F0 ATP synthase subunit C superfamily
3 78 SUPERFAMILY SSF81333 F1F0 ATP synthase subunit C
3 78 InterPro IPR035921 F/V-ATP synthase subunit C superfamily
32 51 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
20 76 NCBIfam TIGR01260 ATP synthase F0 subunit C
20 76 InterPro IPR005953 ATP synthase, F0 complex, subunit C, bacterial/chloroplast
10 32 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
9 74 Hamap MF_01396 ATP synthase subunit c [atpH].
9 74 InterPro IPR000454 ATP synthase, F0 complex, subunit C
1 5 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
9 73 CDD cd18185 ATP-synt_Fo_c_ATPE
10 72 Pfam PF00137 ATP synthase subunit C
10 72 InterPro IPR002379 V-ATPase proteolipid subunit C-like domain
53 75 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
39 60 ProSitePatterns PS00605 ATP synthase c subunit signature.
39 60 InterPro IPR020537 ATP synthase, F0 complex, subunit C, DCCD-binding site
2 77 FunFam G3DSA:1.20.20.10:FF:000002 ATP synthase subunit c
11 30 PRINTS PR00124 ATP synthase C subunit signature
11 30 InterPro IPR000454 ATP synthase, F0 complex, subunit C
32 47 PRINTS PR00124 ATP synthase C subunit signature
32 47 InterPro IPR000454 ATP synthase, F0 complex, subunit C
49 74 PRINTS PR00124 ATP synthase C subunit signature
49 74 InterPro IPR000454 ATP synthase, F0 complex, subunit C
52 76 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
77 85 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
6 31 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA5559
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 0.95
2 0.464

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

55 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
CVM
2WIE
A5HEI4 480.6 Da LogP -1.62 TPSA 178.5 2 viol. ✓ Clean C1CCC(CC1)CCCCO[C@H]2[C@@H]([C@H]([C@@H]([C@H](…
LFA
6TQJ
P69447 282.6 Da LogP 8.05 TPSA 0.0 1 viol. ✓ Clean CCCCCCCCCCCCCCCCCCCC
OLC
6TQJ
P69447 356.5 Da LogP 4.92 TPSA 66.8 ✓ Ro5 ✓ Clean CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](CO)O
YT3
3V3C
P08212 88.9 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Y+3]

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.