Protein profile

KP13_04247

Signal transduction histidine kinase

Genome: KpKP13

Gene: AHE45479.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQJ4
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Amino acids 490
Annotations 9
Features 39
PDB binders 4
Druggability 0.839

Overview

Basic information about this protein and its source genome.

Accession
KP13_04247
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45479.1
Status
annotated
Amino acids
490
Structure source
AlphaFold + ColabFold
EC
2.7.13.3
GO
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: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:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor). GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0000156 Responds to a phosphorelay sensor to initiate a change in cell state or activity. The activity of the response regulator is regulated by transfer of a phosphate from a histidine residue in the sensor, to an aspartate residue in the response regulator. Many but not all response regulators act as transcriptional regulators to elicit a response.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
CytoplasmicMembrane
ColabFold pLDDT
85.27

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 0.839
Structure A0A0H3GQJ4
Pocket Pocket 16
P2Rank 0.551
Structure A0A0H3GQJ4
Pocket Pocket 1
ColabFold model
FPocket 0.998 · Pocket 33
P2Rank 0.853 · Pocket 1
Core conservation Accessory gene
Roary core
CoreCruncher accessory
Gut microbiome 50 / 4744 genomes with a hit
Normalized 0.011

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: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: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:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0000156 Responds to a phosphorelay sensor to initiate a change in cell state or activity. The activity of the response regulator is regulated by transfer of a phosphate from a histidine residue in the sensor, to an aspartate residue in the response regulator. Many but not all response regulators act as transcriptional regulators to elicit a response.
  • GO:0030295 Binds to and increases the activity of a protein kinase, an enzyme which phosphorylates a protein.
  • GO:0007234 The series of molecular signals generated in response to osmotic change, as mediated through a phosphorelay system. In S.cerevisiae, the osmosensor is the histidine kinase Sln1.

Sequence Features

Domain/signature hits from InterPro and related databases.

39 records
Show feature table
Start End DB Term Name
269 336 Pfam PF00512 His Kinase A (phospho-acceptor) domain
269 336 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
341 490 Gene3D G3DSA:3.30.565.10 -
341 490 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
266 332 CDD cd00082 HisKA
266 332 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
382 490 SMART SM00387 HKATPase_4
382 490 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
10 32 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
204 490 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
251 337 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
251 337 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
180 202 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
11 22 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
28 176 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 28 SignalP_GRAM_POSITIVE SignalP-TM SignalP-TM
326 490 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
326 490 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
264 337 FunFam G3DSA:1.10.287.130:FF:000001 Two-component sensor histidine kinase
268 336 SMART SM00388 HisKA_10
268 336 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
387 487 CDD cd00075 HATPase
275 490 ProSiteProfiles PS50109 Histidine kinase domain profile.
275 490 InterPro IPR005467 Histidine kinase domain
384 490 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
384 490 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
1 10 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
221 490 PANTHER PTHR43711 TWO-COMPONENT HISTIDINE KINASE
177 203 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
206 336 Gene3D G3DSA:1.10.287.130 -
23 27 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
1 28 SignalP_EUK SignalP-noTM SignalP-noTM
419 433 PRINTS PR00344 Bacterial sensor protein C-terminal signature
419 433 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
453 471 PRINTS PR00344 Bacterial sensor protein C-terminal signature
453 471 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
476 489 PRINTS PR00344 Bacterial sensor protein C-terminal signature
476 489 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
1 27 Phobius SIGNAL_PEPTIDE Signal peptide region

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_A0A0H3GQJ4
AlphaFold — — full sequence — Viewing
ColabFold KP13_04247
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
16 0.839
36 0.468
33 0.269
13 0.217

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 3.25 0.113
2 2.78 0.085
3 1.81 0.034
4 1.58 0.024
5 1.17 0.01

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
1ID0
P23837 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
PG0
5UKV
P71815 120.1 Da LogP -0.36 TPSA 38.7 ✓ Ro5 ✓ Clean COCCOCCO

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.