Protein profile

KP13_04593

putative signal transduction histidine kinase

Genome: KpKP13

Gene: AHE44468.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQ51
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Amino acids 435
Annotations 8
Features 38
PDB binders 2
Druggability 0.936

Overview

Basic information about this protein and its source genome.

Accession
KP13_04593
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE44468.1
Status
annotated
Amino acids
435
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:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor). 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: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.

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
83.29

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 0.936
Structure A0A0H3GQ51
Pocket Pocket 2
P2Rank 0.807
Structure A0A0H3GQ51
Pocket Pocket 1
ColabFold model
FPocket 0.975 · Pocket 13
P2Rank 0.841 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 26 / 4744 genomes with a hit
Normalized 0.005

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: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: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: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:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records
Show feature table
Start End DB Term Name
1 15 Phobius SIGNAL_PEPTIDE Signal peptide region
86 420 PANTHER PTHR44936 SENSOR PROTEIN CREC
160 213 ProSiteProfiles PS50885 HAMP domain profile.
160 213 InterPro IPR003660 HAMP domain
313 423 SMART SM00387 HKATPase_4
313 423 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
160 435 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
137 159 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
221 423 ProSiteProfiles PS50109 Histidine kinase domain profile.
221 423 InterPro IPR005467 Histidine kinase domain
318 419 CDD cd00075 HATPase
160 213 SMART SM00304 HAMP_11
212 268 CDD cd00082 HisKA
212 268 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
272 419 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
272 419 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
2 10 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
139 159 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
316 419 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
316 419 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
157 266 Gene3D G3DSA:1.10.287.130 -
214 272 SMART SM00388 HisKA_10
214 272 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
1 1 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
295 423 Gene3D G3DSA:3.30.565.10 -
295 423 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
1 17 SignalP_EUK SignalP-noTM SignalP-noTM
16 138 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
11 15 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
198 270 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
198 270 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
4 21 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
348 362 PRINTS PR00344 Bacterial sensor protein C-terminal signature
348 362 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
383 401 PRINTS PR00344 Bacterial sensor protein C-terminal signature
383 401 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
366 376 PRINTS PR00344 Bacterial sensor protein C-terminal signature
366 376 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal

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_A0A0H3GQ51
AlphaFold — — full sequence — Viewing
ColabFold KP13_04593
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
2 0.936
1 0.544

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 13.22 0.678

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)…
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.