Protein profile

PA3191

two-component sensor

Genome: NC_002516.2

Gene: gtrS PA3191 Structure source: AlphaFold UniProt Q9HZ47
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Amino acids 473
Annotations 8
Features 47
PDB binders 4
Druggability 0.866

Overview

Basic information about this protein and its source genome.

Accession
PA3191
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
gtrS PA3191
Status
annotated
Amino acids
473
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: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 0.866
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.

47 records
Show feature table
Start End DB Term Name
198 218 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
219 473 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
328 469 Gene3D G3DSA:3.30.565.10 -
328 469 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
1 24 Phobius SIGNAL_PEPTIDE Signal peptide region
220 262 Gene3D G3DSA:1.10.8.500 HAMP domain in histidine kinase
1 20 SignalP_EUK SignalP-TM SignalP-TM
331 469 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
331 469 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
10 32 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
270 328 SMART SM00388 HisKA_10
270 328 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
214 265 Pfam PF00672 HAMP domain
214 265 InterPro IPR003660 HAMP domain
277 471 ProSiteProfiles PS50109 Histidine kinase domain profile.
277 471 InterPro IPR005467 Histidine kinase domain
219 267 SUPERFAMILY SSF158472 HAMP domain-like
371 467 CDD cd00075 HATPase
254 313 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
254 313 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
455 468 PRINTS PR00344 Bacterial sensor protein C-terminal signature
455 468 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
418 428 PRINTS PR00344 Bacterial sensor protein C-terminal signature
418 428 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
400 414 PRINTS PR00344 Bacterial sensor protein C-terminal signature
400 414 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
431 449 PRINTS PR00344 Bacterial sensor protein C-terminal signature
431 449 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
366 471 SMART SM00387 HKATPase_4
366 471 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
217 269 SMART SM00304 HAMP_11
217 269 InterPro IPR003660 HAMP domain
3 468 PANTHER PTHR44936 SENSOR PROTEIN CREC
25 197 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
268 309 CDD cd00082 HisKA
268 309 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
263 324 Gene3D G3DSA:1.10.287.130 -
10 20 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
367 468 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
367 468 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
198 220 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
217 269 ProSiteProfiles PS50885 HAMP domain profile.
271 313 Pfam PF00512 His Kinase A (phospho-acceptor) domain
271 313 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
1 9 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
220 264 CDD cd06225 HAMP
21 24 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.

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

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 PA3191
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
8 0.866
1 0.855
2 0.764
25 0.257

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.

54 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)…
EMC
3A0W
Q9X180 229.7 Da LogP 0.97 TPSA 0.0 ✓ Ro5 ✓ Clean CC[Hg+]
EMT
3A0W
Q9X180 382.8 Da LogP 2.91 TPSA 37.3 ✓ Ro5 ✓ Clean CC[Hg]Sc1ccccc1C(=O)O
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.