Protein profile

PA5555

ATP synthase subunit gamma

Genome: NC_002516.2

Gene: PA5555 atpG Structure source: AlphaFold UniProt Q9HT19
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Amino acids 286
Annotations 7
Features 25
PDB binders 4

Overview

Basic information about this protein and its source genome.

Accession
PA5555
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5555 atpG
Status
annotated
Amino acids
286
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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. 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: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).

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
29.866
Human E-value
8.24e-28
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

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: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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • 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: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).
  • GO:0045261 OBSOLETE. 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records
Show feature table
Start End DB Term Name
2 286 SUPERFAMILY SSF52943 ATP synthase (F1-ATPase), gamma subunit
2 286 InterPro IPR035968 ATP synthase, F1 complex, gamma subunit superfamily
27 245 Gene3D G3DSA:3.40.1380.10 -
1 286 NCBIfam TIGR01146 ATP synthase F1 subunit gamma
1 286 InterPro IPR000131 ATP synthase, F1 complex, gamma subunit
2 283 CDD cd12151 F1-ATPase_gamma
2 283 InterPro IPR000131 ATP synthase, F1 complex, gamma subunit
272 285 ProSitePatterns PS00153 ATP synthase gamma subunit signature.
272 285 InterPro IPR023632 ATP synthase, F1 complex, gamma subunit conserved site
1 286 Hamap MF_00815 ATP synthase gamma chain [atpG].
2 285 PANTHER PTHR11693 ATP SYNTHASE GAMMA CHAIN
2 285 InterPro IPR000131 ATP synthase, F1 complex, gamma subunit
27 245 FunFam G3DSA:3.40.1380.10:FF:000001 ATP synthase gamma chain
5 283 Gene3D G3DSA:1.10.287.80 ATP synthase, gamma subunit, helix hairpin domain
264 285 PRINTS PR00126 ATP synthase gamma subunit signature
264 285 InterPro IPR000131 ATP synthase, F1 complex, gamma subunit
233 252 PRINTS PR00126 ATP synthase gamma subunit signature
233 252 InterPro IPR000131 ATP synthase, F1 complex, gamma subunit
166 183 PRINTS PR00126 ATP synthase gamma subunit signature
166 183 InterPro IPR000131 ATP synthase, F1 complex, gamma subunit
73 92 PRINTS PR00126 ATP synthase gamma subunit signature
73 92 InterPro IPR000131 ATP synthase, F1 complex, gamma subunit
196 286 FunFam G3DSA:1.10.287.80:FF:000005 ATP synthase gamma chain
5 285 Pfam PF00231 ATP synthase
5 285 InterPro IPR000131 ATP synthase, F1 complex, gamma subunit

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

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA5555
AlphaFold — — full sequence — Viewing

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
ANP
2JIZ
P05631 506.2 Da LogP -2.06 TPSA 281.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
AZI
2JIZ
P05631 42.0 Da LogP 0.87 TPSA 58.7 ✓ Ro5 Alert [N-]=[N+]=[N-]
QUE
2JJ2
P05631 302.2 Da LogP 1.99 TPSA 131.4 ✓ Ro5 Alert c1cc(c(cc1C2=C(C(=O)c3c(cc(cc3O2)O)O)O)O)O
STL
2JIZ
P05631 228.2 Da LogP 2.97 TPSA 60.7 ✓ Ro5 ✓ Clean c1cc(ccc1\C=C\c2cc(cc(c2)O)O)O

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.