Protein profile

KP13_02788

Sensor protein qseC

Genome: KpKP13

Gene: qseC AHE42643.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GYJ2
Amino acids 449
Annotations 7
Features 38
PDB binders 3
Druggability 0.762

Overview

Basic information about this protein and its source genome.

Accession
KP13_02788
Gene
qseC AHE42643.1
Status
annotated
Amino acids
449
Structure source
AlphaFold + ColabFold
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: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.

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
86.25

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 0.762
Structure A0A0H3GYJ2
Pocket Pocket 4
P2Rank 0.614
Structure A0A0H3GYJ2
Pocket Pocket 1
ColabFold model
FPocket 0.904 · Pocket 40
P2Rank 0.768 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 90 / 4744 genomes with a hit
Normalized 0.019

Sequence

Primary amino-acid sequence viewer.

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: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: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
25 32 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
236 298 CDD cd00082 HisKA
236 298 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
13 24 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
276 449 FunFam G3DSA:3.30.565.10:FF:000055 Two-component sensor histidine kinase
13 35 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
306 449 Gene3D G3DSA:3.30.565.10 -
306 449 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
243 449 ProSiteProfiles PS50109 Histidine kinase domain profile.
243 449 InterPro IPR005467 Histidine kinase domain
1 12 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
33 163 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
291 448 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
291 448 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
236 302 SMART SM00388 HisKA_10
236 302 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
164 182 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
219 301 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
219 301 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
187 301 FunFam G3DSA:1.10.287.130:FF:000035 Two-component sensor histidine kinase
183 449 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
348 449 SMART SM00387 HKATPase_4
348 449 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
238 301 Pfam PF00512 His Kinase A (phospho-acceptor) domain
238 301 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
159 181 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
3 447 PANTHER PTHR45436 SENSOR HISTIDINE KINASE YKOH
413 431 PRINTS PR00344 Bacterial sensor protein C-terminal signature
413 431 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
381 395 PRINTS PR00344 Bacterial sensor protein C-terminal signature
381 395 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
353 445 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
353 445 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
128 185 Gene3D G3DSA:1.20.5.1040 Sensor protein qsec.
1 60 Gene3D G3DSA:1.20.5.1040 Sensor protein qsec.
187 302 Gene3D G3DSA:1.10.287.130 -
1 32 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_A0A0H3GYJ2
AlphaFold full sequence Viewing
ColabFold KP13_02788
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
4 0.762
29 0.61

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 6.97 0.36
2 1.01 0.006
3 0.93 0.004

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.