Protein profile

PA5054

ATP-dependent protease ATP-binding subunit HslU

Genome: NC_002516.2

Gene: PA5054 hslU Structure source: AlphaFold UniProt Q9HUC5
Export view
Amino acids 447
Annotations 7
Features 24
PDB binders 2
Druggability 0.589

Overview

Basic information about this protein and its source genome.

Accession
PA5054
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5054 hslU
Status
annotated
Amino acids
447
Structure source
AlphaFold
GO
GO:0009376 A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. GO:0008233 Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. GO:0036402 Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome. GO:0043335 The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
27.881
Human E-value
1.51e-16
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

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 0.589
Structure –
Pocket –

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:0009376 A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
  • GO:0008233 Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
  • GO:0036402 Catalysis of the reaction: ATP + H2O = ADP + phosphate, which promotes unfolding of protein substrates, and channel opening of the core proteasome.
  • GO:0043335 The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state.
  • GO:0051603 OBSOLETE. The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records
Show feature table
Start End DB Term Name
1 447 Hamap MF_00249 ATP-dependent protease ATPase subunit HslU [hslU].
1 447 InterPro IPR004491 Heat shock protein HslU
187 329 Pfam PF07724 AAA domain (Cdc48 subfamily)
187 329 InterPro IPR003959 ATPase, AAA-type, core
52 137 Pfam PF00004 ATPase family associated with various cellular activities (AAA)
52 137 InterPro IPR003959 ATPase, AAA-type, core
3 312 PANTHER PTHR48102 ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED
145 332 FunFam G3DSA:3.40.50.300:FF:000213 ATP-dependent protease ATPase subunit HslU
3 447 NCBIfam TIGR00390 HslU--HslV peptidase ATPase subunit
3 447 InterPro IPR004491 Heat shock protein HslU
48 332 SMART SM00382 AAA_5
48 332 InterPro IPR003593 AAA+ ATPase domain
149 332 Gene3D G3DSA:3.40.50.300 -
149 332 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
1 138 Gene3D G3DSA:3.40.50.300 -
1 138 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
109 181 FunFam G3DSA:1.10.8.10:FF:000028 ATP-dependent protease ATPase subunit HslU
335 433 SMART SM01086 ClpB_D2_small_2
335 433 InterPro IPR019489 Clp ATPase, C-terminal
335 444 Gene3D G3DSA:1.10.8.60 -
3 445 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
3 445 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
4 332 CDD cd19498 RecA-like_HslU
1 113 FunFam G3DSA:3.40.50.300:FF:000220 ATP-dependent protease ATPase subunit HslU

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 + 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 PA5054
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 0.589

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.

52 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
AGS
4I81
P0A6H1 523.2 Da LogP -1.51 TPSA 262.1 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
ANP
1DO2
P0A6H5 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)…

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.