Protein profile

PA1798

two-component sensor ParS

Genome: NC_002516.2

Gene: parS PA1798 Structure source: Experimental + AlphaFold UniProt Q9I2U4
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Amino acids 428
Annotations 8
Features 45
PDB binders 3
Druggability 0.882

Overview

Basic information about this protein and its source genome.

Accession
PA1798
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
parS PA1798
Status
annotated
Amino acids
428
Structure source
Experimental + AlphaFold
EC
2.7.13.3
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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0000155 Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
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 0.882
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0000155 Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
  • GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
  • GO:0016310 The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

Sequence Features

Domain/signature hits from InterPro and related databases.

45 records
Show feature table
Start End DB Term Name
158 206 SUPERFAMILY SSF158472 HAMP domain-like
323 426 CDD cd16939 HATPase_RstB-like
132 154 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
209 273 Pfam PF00512 His Kinase A (phospho-acceptor) domain
209 273 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
154 202 CDD cd06225 HAMP
208 273 SMART SM00388 HisKA_10
208 273 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
371 381 PRINTS PR00344 Bacterial sensor protein C-terminal signature
371 381 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
388 406 PRINTS PR00344 Bacterial sensor protein C-terminal signature
388 406 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
353 367 PRINTS PR00344 Bacterial sensor protein C-terminal signature
353 367 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
1 19 Phobius SIGNAL_PEPTIDE Signal peptide region
154 200 Gene3D G3DSA:1.10.8.500 HAMP domain in histidine kinase
1 3 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
155 428 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
191 274 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
191 274 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
201 269 Gene3D G3DSA:1.10.287.130 -
209 269 CDD cd00082 HisKA
209 269 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
158 203 Pfam PF00672 HAMP domain
158 203 InterPro IPR003660 HAMP domain
1 19 SignalP_EUK SignalP-TM SignalP-TM
4 14 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
2 425 PANTHER PTHR44936 SENSOR PROTEIN CREC
20 132 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
263 424 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
263 424 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
321 425 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
321 425 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
133 154 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
155 207 ProSiteProfiles PS50885 HAMP domain profile.
155 207 InterPro IPR003660 HAMP domain
5 27 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
215 428 ProSiteProfiles PS50109 Histidine kinase domain profile.
215 428 InterPro IPR005467 Histidine kinase domain
155 207 SMART SM00304 HAMP_11
15 19 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
277 426 Gene3D G3DSA:3.30.565.10 -
277 426 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
318 428 SMART SM00387 HKATPase_4
318 428 InterPro IPR003594 Histidine kinase/HSP90-like ATPase

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

1 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 8JU7
X-ray 1.80 Å A,B
24.1% 29-131
PDBe RCSB PDBj File
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AlphaFold PA1798
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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.

53 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
4BIW
P0AE82 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)…
PG0
5UKV
P71815 120.1 Da LogP -0.36 TPSA 38.7 ✓ Ro5 ✓ Clean COCCOCCO
RDC
3CGY
P0DM80 364.8 Da LogP 2.69 TPSA 96.4 ✓ Ro5 ✓ Clean C[C@@H]1C[C@@H]2[C@H](O2)\C=C/C=C/C(=O)Cc3c(c(c…

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.