Protein profile

KP13_00019

ATP synthase subunit a

Genome: KpKP13

Gene: AHE47128.1 atpB Structure source: AlphaFold + ColabFold UniProt A0A0H3H0K2
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Amino acids 271
Annotations 7
Features 38
PDB binders 1
Druggability 0.985

Overview

Basic information about this protein and its source genome.

Accession
KP13_00019
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE47128.1 atpB
Status
annotated
Amino acids
271
Structure source
AlphaFold + ColabFold
GO
GO:0015078 Enables the transfer of a proton from one side of a membrane to the other. 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: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).

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 (%)
91.882
DEG E-value
2.5999999999999997e-177
Localization
CytoplasmicMembrane
ColabFold pLDDT
57.81

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 0.985
Structure A0A0H3H0K2
Pocket Pocket 9
P2Rank 0.868
Structure A0A0H3H0K2
Pocket Pocket 1
ColabFold model
FPocket 0.985 · Pocket 30
P2Rank 0.707 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 177 / 4744 genomes with a hit
Normalized 0.037

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7
  • GO:0015078 Enables the transfer of a proton from one side of a membrane to the other.
  • 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: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:0042777 The chemical reactions and pathways resulting in the formation of ATP driven by transport of protons across a plasma membrane to generate an electrochemical gradient (proton-motive force).

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records
Show feature table
Start End DB Term Name
22 271 PANTHER PTHR42823 ATP SYNTHASE SUBUNIT A, CHLOROPLASTIC
22 271 InterPro IPR045082 ATP synthase, F0 complex, subunit A, bacterial/chloroplast
206 215 ProSitePatterns PS00449 ATP synthase a subunit signature.
206 215 InterPro IPR023011 ATP synthase, F0 complex, subunit A, active site
38 266 NCBIfam TIGR01131 F0F1 ATP synthase subunit A
38 266 InterPro IPR000568 ATP synthase, F0 complex, subunit A
265 271 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
100 118 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
12 271 Hamap MF_01393 ATP synthase subunit a [atpB].
12 271 InterPro IPR000568 ATP synthase, F0 complex, subunit A
211 233 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
36 60 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
1 35 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
61 99 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
36 58 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
234 238 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
95 265 SUPERFAMILY SSF81336 F1F0 ATP synthase subunit A
95 265 InterPro IPR035908 ATP synthase, F0 complex, subunit A superfamily
100 122 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
167 210 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
142 164 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
102 265 CDD cd00310 ATP-synt_Fo_a_6
147 166 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
239 264 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
119 146 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
95 271 Gene3D G3DSA:1.20.120.220 ATP synthase, F0 complex, subunit A
95 271 InterPro IPR035908 ATP synthase, F0 complex, subunit A superfamily
95 271 FunFam G3DSA:1.20.120.220:FF:000002 ATP synthase subunit a
211 233 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
243 265 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
203 225 PRINTS PR00123 ATP synthase A subunit signature
203 225 InterPro IPR000568 ATP synthase, F0 complex, subunit A
251 266 PRINTS PR00123 ATP synthase A subunit signature
251 266 InterPro IPR000568 ATP synthase, F0 complex, subunit A
104 120 PRINTS PR00123 ATP synthase A subunit signature
104 120 InterPro IPR000568 ATP synthase, F0 complex, subunit A
47 265 Pfam PF00119 ATP synthase A chain
47 265 InterPro IPR000568 ATP synthase, F0 complex, subunit A

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

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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_A0A0H3H0K2
AlphaFold — — full sequence — Viewing
ColabFold KP13_00019
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
9 0.985
31 0.53
5 0.245

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 14.74 0.733
2 11.52 0.614
3 5.47 0.26
4 5.28 0.247
5 4.5 0.192

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

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
BQ1
7JGC
A0R206 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.