Protein profile

PA1180

two-component sensor PhoQ

Genome: NC_002516.2

Gene: PA1180 phoQ Structure source: AlphaFold UniProt Q9I4F8
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Amino acids 448
Annotations 9
Features 36
PDB binders 3
Druggability 0.934

Overview

Basic information about this protein and its source genome.

Accession
PA1180
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1180 phoQ
Status
annotated
Amino acids
448
Structure source
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:0000160 A conserved series of molecular signals found in prokaryotes and eukaryotes; involves autophosphorylation of a histidine kinase and the transfer of the phosphate group to an aspartate that then acts as a phospho-donor to response regulator proteins. 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.

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 0.934
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • 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:0000160 A conserved series of molecular signals found in prokaryotes and eukaryotes; involves autophosphorylation of a histidine kinase and the transfer of the phosphate group to an aspartate that then acts as a phospho-donor to response regulator proteins.
  • 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.

36 records
Show feature table
Start End DB Term Name
243 295 CDD cd00082 HisKA
243 295 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
34 165 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 446 PANTHER PTHR45436 SENSOR HISTIDINE KINASE YKOH
7 29 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
1 10 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
190 448 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
186 294 FunFam G3DSA:1.10.287.130:FF:000013 Sensor histidine kinase PhoQ
26 33 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
11 25 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
347 445 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
347 445 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
311 445 CDD cd16954 HATPase_PhoQ-like
378 392 PRINTS PR00344 Bacterial sensor protein C-terminal signature
378 392 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
409 427 PRINTS PR00344 Bacterial sensor protein C-terminal signature
409 427 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
238 300 SMART SM00388 HisKA_10
238 300 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
343 448 SMART SM00387 HKATPase_4
343 448 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
186 237 ProSiteProfiles PS50885 HAMP domain profile.
186 237 InterPro IPR003660 HAMP domain
308 445 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
308 445 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
245 448 ProSiteProfiles PS50109 Histidine kinase domain profile.
245 448 InterPro IPR005467 Histidine kinase domain
1 33 Phobius SIGNAL_PEPTIDE Signal peptide region
302 447 FunFam G3DSA:3.30.565.10:FF:000083 Two-component sensor histidine kinase
166 189 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
190 299 Gene3D G3DSA:1.10.287.130 -
167 189 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
221 292 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
221 292 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
302 447 Gene3D G3DSA:3.30.565.10 -
302 447 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily

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

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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 PA1180
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
16 0.855
12 0.726
3 0.263
1 0.236

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.