Protein profile

KP13_04870

Sensor protein phoQ

Genome: KpKP13

Gene: AHE45230.1 phoQ Structure source: AlphaFold + ColabFold UniProt A0A0H3GLK4
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Amino acids 488
Annotations 13
Features 35
PDB binders 2
Druggability 0.366

Overview

Basic information about this protein and its source genome.

Accession
KP13_04870
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45230.1 phoQ
Status
annotated
Amino acids
488
Structure source
AlphaFold + ColabFold
EC
2.7.13.3
GO
GO:0018106 The phosphorylation of peptidyl-histidine to form peptidyl-1'-phospho-L-histidine (otherwise known as tau-phosphohistidine, tele-phosphohistidine) or peptidyl-3'-phospho-L-histidine (otherwise known as pi-phosphohistidine, pros-phosphohistidine). 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. GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor). GO:0004673 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine. GO:0046872 Binding to a metal ion. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
80.698
DEG E-value
0.0
Localization
CytoplasmicMembrane
ColabFold pLDDT
84.07

Selected Druggability evidence

AlphaFold / UniProt model

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 0.366
Structure A0A0H3GLK4
Pocket Pocket 6
P2Rank 0.805
Structure A0A0H3GLK4
Pocket Pocket 1
ColabFold model
FPocket 0.809 · Pocket 28
P2Rank 0.849 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 108 / 4744 genomes with a hit
Normalized 0.023

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 12 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

12
  • GO:0018106 The phosphorylation of peptidyl-histidine to form peptidyl-1'-phospho-L-histidine (otherwise known as tau-phosphohistidine, tele-phosphohistidine) or peptidyl-3'-phospho-L-histidine (otherwise known as pi-phosphohistidine, pros-phosphohistidine).
  • 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.
  • GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
  • GO:0004673 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine.
  • GO:0046872 Binding to a metal ion.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • 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: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: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:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
  • GO:0004721 Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity.

Sequence Features

Domain/signature hits from InterPro and related databases.

35 records
Show feature table
Start End DB Term Name
343 478 CDD cd16954 HATPase_PhoQ-like
194 216 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
215 324 Gene3D G3DSA:1.10.287.130 -
337 478 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
337 478 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
10 189 Pfam PF08918 PhoQ Sensor
10 189 InterPro IPR015014 PhoQ Sensor domain
1 19 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
272 325 CDD cd00082 HisKA
272 325 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
194 216 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
10 486 PANTHER PTHR45436 SENSOR HISTIDINE KINASE YKOH
332 487 Gene3D G3DSA:3.30.565.10 -
332 487 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
215 324 FunFam G3DSA:1.10.287.130:FF:000013 Sensor histidine kinase PhoQ
215 266 ProSiteProfiles PS50885 HAMP domain profile.
215 266 InterPro IPR003660 HAMP domain
44 196 Gene3D G3DSA:3.30.450.140 -
44 196 InterPro IPR038429 PhoQ Sensor superfamily
274 482 ProSiteProfiles PS50109 Histidine kinase domain profile.
274 482 InterPro IPR005467 Histidine kinase domain
20 43 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
44 193 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
250 323 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
250 323 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
217 488 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
375 482 SMART SM00387 HKATPase_4
375 482 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
442 460 PRINTS PR00344 Bacterial sensor protein C-terminal signature
442 460 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
411 425 PRINTS PR00344 Bacterial sensor protein C-terminal signature
411 425 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
20 42 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
376 475 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
376 475 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.

3D visualization script Full viewer

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Structural evidence

0 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GLK4
AlphaFold — — full sequence — Viewing
ColabFold KP13_04870
ColabFold — — full sequence — Loaded
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
6 0.366
1 0.252

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 11.57 0.616
2 0.95 0.005

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.

52 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)…
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.