Protein profile

KP13_01999

Sensor protein creC

Genome: KpKP13

Gene: creC AHE46436.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GHZ7
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Amino acids 474
Annotations 7
Features 40
PDB binders 4
Druggability 0.857

Overview

Basic information about this protein and its source genome.

Accession
KP13_01999
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
creC AHE46436.1
Status
annotated
Amino acids
474
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
90.77

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 0.857
Structure A0A0H3GHZ7
Pocket Pocket 1
P2Rank 0.849
Structure A0A0H3GHZ7
Pocket Pocket 1
ColabFold model
FPocket 0.842 · Pocket 1
P2Rank 0.886 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 68 / 4744 genomes with a hit
Normalized 0.014

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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

40 records
Show feature table
Start End DB Term Name
51 172 SUPERFAMILY SSF103190 Sensory domain-like
51 172 InterPro IPR029151 Periplasmic sensor-like domain superfamily
311 469 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
311 469 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
28 183 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
5 27 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
207 474 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
317 471 Gene3D G3DSA:3.30.565.10 -
317 471 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
6 27 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
240 319 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
240 319 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
1 5 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
49 166 Gene3D G3DSA:3.30.450.20 PAS domain
184 206 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
255 320 SMART SM00388 HisKA_10
255 320 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
363 470 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
363 470 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
256 316 FunFam G3DSA:1.10.287.130:FF:000051 Two-component system sensor histidine kinase CreC
204 255 ProSiteProfiles PS50885 HAMP domain profile.
204 255 InterPro IPR003660 HAMP domain
254 316 CDD cd00082 HisKA
254 316 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
210 316 Gene3D G3DSA:1.10.287.130 -
184 206 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
2 471 PANTHER PTHR45436 SENSOR HISTIDINE KINASE YKOH
400 414 PRINTS PR00344 Bacterial sensor protein C-terminal signature
400 414 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
433 451 PRINTS PR00344 Bacterial sensor protein C-terminal signature
433 451 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
418 428 PRINTS PR00344 Bacterial sensor protein C-terminal signature
418 428 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
260 319 Pfam PF00512 His Kinase A (phospho-acceptor) domain
260 319 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
42 166 CDD cd18773 PDC1_HK_sensor
363 473 SMART SM00387 HKATPase_4
363 473 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
262 473 ProSiteProfiles PS50109 Histidine kinase domain profile.
262 473 InterPro IPR005467 Histidine kinase domain

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_A0A0H3GHZ7
AlphaFold — — full sequence — Viewing
ColabFold KP13_01999
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
1 0.857
45 0.752

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 15.76 0.761
2 3.85 0.15
3 1.45 0.02
4 1.02 0.006

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
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)…
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.