Protein profile

PA0757

two-component sensor

Genome: NC_002516.2

Gene: PA0757 Structure source: AlphaFold UniProt Q9I5H2
Amino acids 460
Annotations 8
Features 44
PDB binders 3
Druggability 0.429

Overview

Basic information about this protein and its source genome.

Accession
PA0757
Gene
PA0757
Status
annotated
Amino acids
460
Structure source
AlphaFold
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: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).

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 0.429
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: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.

44 records
Show feature table
Start End DB Term Name
195 309 Gene3D G3DSA:1.10.287.130 -
1 458 PANTHER PTHR45436 SENSOR HISTIDINE KINASE YKOH
373 457 CDD cd00075 HATPase
172 194 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
244 309 SMART SM00388 HisKA_10
244 309 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
251 460 ProSiteProfiles PS50109 Histidine kinase domain profile.
251 460 InterPro IPR005467 Histidine kinase domain
1 27 SignalP_EUK SignalP-TM SignalP-TM
245 309 Pfam PF00512 His Kinase A (phospho-acceptor) domain
245 309 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
357 460 SMART SM00387 HKATPase_4
357 460 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
19 167 Pfam PF08521 Two-component sensor kinase N-terminal
19 167 InterPro IPR013727 Two-component sensor kinase, N-terminal
10 32 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
11 25 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
312 459 Gene3D G3DSA:3.30.565.10 -
312 459 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
359 459 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
359 459 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
195 460 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1 30 Phobius SIGNAL_PEPTIDE Signal peptide region
191 239 Pfam PF00672 HAMP domain
191 239 InterPro IPR003660 HAMP domain
298 459 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
298 459 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
243 305 CDD cd00082 HisKA
243 305 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
1 10 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
227 309 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
227 309 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
26 30 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
409 419 PRINTS PR00344 Bacterial sensor protein C-terminal signature
409 419 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
421 439 PRINTS PR00344 Bacterial sensor protein C-terminal signature
421 439 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
391 405 PRINTS PR00344 Bacterial sensor protein C-terminal signature
391 405 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
31 171 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
240 310 FunFam G3DSA:1.10.287.130:FF:000001 Two-component sensor histidine kinase
172 194 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
191 243 ProSiteProfiles PS50885 HAMP domain profile.
191 243 InterPro IPR003660 HAMP domain

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 PA0757
AlphaFold full sequence Viewing
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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
2 0.353

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 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 P71815 120.1 Da LogP -0.36 TPSA 38.7 ✓ Ro5 ✓ Clean COCCOCCO
RDC 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.