Protein profile

KP13_00020

ATP synthase subunit c

Genome: KpKP13

Gene: atpE AHE47129.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GVB8
Amino acids 79
Annotations 9
Features 27
PDB binders 0
Druggability 0.487

Overview

Basic information about this protein and its source genome.

Accession
KP13_00020
Gene
atpE AHE47129.1
Status
annotated
Amino acids
79
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
100.0
DEG E-value
3.24e-49
Localization
CytoplasmicMembrane
ColabFold pLDDT
92.32

Selected Druggability evidence

AlphaFold / UniProt model

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 0.487
Structure A0A0H3GVB8
Pocket Pocket 4
P2Rank
Structure A0A0H3GVB8
Pocket No pockets
ColabFold model
FPocket 0.213 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 224 / 4744 genomes with a hit
Normalized 0.047

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:0015078 Enables the transfer of a proton from one side of a membrane to the other.
  • GO:1902600 The directed movement of a proton across a membrane.
  • 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:0045263 OBSOLETE. All non-F1 subunits of a hydrogen-transporting ATP synthase, including integral and peripheral membrane proteins.
  • 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: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: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).

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records
Show feature table
Start End DB Term Name
10 75 Hamap MF_01396 ATP synthase subunit c [atpH].
10 75 InterPro IPR000454 ATP synthase, F0 complex, subunit C
1 11 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
10 73 CDD cd18185 ATP-synt_Fo_c_ATPE
77 79 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
53 75 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
10 32 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
12 32 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
11 71 Pfam PF00137 ATP synthase subunit C
11 71 InterPro IPR002379 V-ATPase proteolipid subunit C-like domain
3 77 SUPERFAMILY SSF81333 F1F0 ATP synthase subunit C
3 77 InterPro IPR035921 F/V-ATP synthase subunit C superfamily
12 31 PRINTS PR00124 ATP synthase C subunit signature
12 31 InterPro IPR000454 ATP synthase, F0 complex, subunit C
50 75 PRINTS PR00124 ATP synthase C subunit signature
50 75 InterPro IPR000454 ATP synthase, F0 complex, subunit C
33 48 PRINTS PR00124 ATP synthase C subunit signature
33 48 InterPro IPR000454 ATP synthase, F0 complex, subunit C
40 61 ProSitePatterns PS00605 ATP synthase c subunit signature.
40 61 InterPro IPR020537 ATP synthase, F0 complex, subunit C, DCCD-binding site
53 76 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
33 52 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1 79 Gene3D G3DSA:1.20.20.10 F1F0 ATP synthase subunit C
1 79 InterPro IPR038662 F1F0 ATP synthase subunit C superfamily
2 79 FunFam G3DSA:1.20.20.10:FF:000002 ATP synthase subunit c
20 77 NCBIfam TIGR01260 ATP synthase F0 subunit C
20 77 InterPro IPR005953 ATP synthase, F0 complex, subunit C, bacterial/chloroplast

3D Structure

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

3D visualization script Full viewer

Loading 3D structure...

Legend High Medium Low

Structural evidence

0 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GVB8
AlphaFold full sequence Viewing
ColabFold KP13_00020
ColabFold full sequence Loaded
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
4 0.487
2 0.252
1 0.238

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.

1 records

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Show only:
Ligand UniProt (homolog) pchembl MW · LogP · TPSA Lipinski PAINS SMILES
BQ1 P00845 6.30 555.5 Da LogP 7.13 TPSA 45.6 2 viol. ✓ Clean CN(C)CC[C@@](c1cccc2c1cccc2)([C@H](c3ccccc3)c4c…

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.