Protein profile

PA3206

two-component sensor

Genome: NC_002516.2

Gene: PA3206 Structure source: AlphaFold UniProt Q9HZ34
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Amino acids 445
Annotations 7
Features 46
PDB binders 3
Druggability 0.672

Overview

Basic information about this protein and its source genome.

Accession
PA3206
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3206
Status
annotated
Amino acids
445
Structure source
AlphaFold
EC
2.7.13.3
GO
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. 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:0046677 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms. 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.

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 0.672
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MRSLFWRILAAFWLALLLVAGLSILLGRALNQDTWIIARHPGLKDLAEQWTALYEEQGSYAAQGLLEQRRRDYGISIQVLDESGQRLVDGTYLPRPHHRPPRTSDRNLPRFPWRQLSQEYVSPQSNHTYLFIYRIPHPELEAWHRGSLLWPLSALGIALVVLTLFSLLLTLSITRPLNRLRRAVHDLGQTAYQKDSLARLARRGDELGTLARDFNRMGERLQSLIGSQRQLLRDVSHELRSPLARLRIALALAERAEPEARAQMWPRLEQECDRLEALIGEILALARLDAEPGASQRIALLPLLQRLREDALLLAPEQDIRLEVAPDLSIDGWPDMFERAVDNLLRNAVRFNPVGQPLEVRASSAGDYLRLSVRDHGPGIAAELQEQLGEPFFRAPNQSSPGHGLGLAIARRAIERHGGHLRLGNHPDGGFIATLSLPLRRKATE

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • 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:0046677 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
  • 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.

46 records
Show feature table
Start End DB Term Name
1 7 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
332 441 SMART SM00387 HKATPase_4
332 441 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
145 227 Gene3D G3DSA:6.10.340.10 -
227 287 CDD cd00082 HisKA
227 287 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
227 291 SMART SM00388 HisKA_10
227 291 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
234 441 ProSiteProfiles PS50109 Histidine kinase domain profile.
234 441 InterPro IPR005467 Histidine kinase domain
171 226 SMART SM00304 HAMP_11
171 226 InterPro IPR003660 HAMP domain
168 222 Pfam PF00672 HAMP domain
168 222 InterPro IPR003660 HAMP domain
174 221 CDD cd06225 HAMP
148 173 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
172 225 SUPERFAMILY SSF158472 HAMP domain-like
281 439 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
281 439 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
2 441 PANTHER PTHR45436 SENSOR HISTIDINE KINASE YKOH
228 290 Gene3D G3DSA:1.10.287.130 -
210 290 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
210 290 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
27 31 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
4 26 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
369 383 PRINTS PR00344 Bacterial sensor protein C-terminal signature
369 383 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
401 419 PRINTS PR00344 Bacterial sensor protein C-terminal signature
401 419 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
425 438 PRINTS PR00344 Bacterial sensor protein C-terminal signature
425 438 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
387 397 PRINTS PR00344 Bacterial sensor protein C-terminal signature
387 397 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
171 226 ProSiteProfiles PS50885 HAMP domain profile.
32 147 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
152 174 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
337 437 CDD cd00075 HATPase
1 31 Phobius SIGNAL_PEPTIDE Signal peptide region
8 26 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
337 440 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
337 440 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
227 290 Pfam PF00512 His Kinase A (phospho-acceptor) domain
227 290 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
294 438 Gene3D G3DSA:3.30.565.10 -
294 438 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
174 445 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.

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 PA3206
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
4 0.672
1 0.391

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.