Protein profile

KP13_03152

Signal transduction histidine-protein kinase baeS

Genome: KpKP13

Gene: baeS AHE43632.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GSM3
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Amino acids 492
Annotations 7
Features 45
PDB binders 3
Druggability 0.371

Overview

Basic information about this protein and its source genome.

Accession
KP13_03152
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
baeS AHE43632.1
Status
annotated
Amino acids
492
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
82.08

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 0.371
Structure A0A0H3GSM3
Pocket Pocket 26
P2Rank 0.865
Structure A0A0H3GSM3
Pocket Pocket 1
ColabFold model
FPocket 0.944 · Pocket 4
P2Rank 0.859 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 94 / 4744 genomes with a hit
Normalized 0.02

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.

45 records
Show feature table
Start End DB Term Name
179 263 Gene3D G3DSA:6.10.340.10 -
264 328 FunFam G3DSA:1.10.287.130:FF:000014 Signal transduction histidine-protein kinase BaeS
13 35 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
248 329 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
248 329 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
265 329 Pfam PF00512 His Kinase A (phospho-acceptor) domain
265 329 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
3 485 PANTHER PTHR45436 SENSOR HISTIDINE KINASE YKOH
215 259 CDD cd06225 HAMP
338 489 Gene3D G3DSA:3.30.565.10 -
338 489 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
374 485 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
374 485 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
101 124 MobiDBLite mobidb-lite consensus disorder prediction
89 129 MobiDBLite mobidb-lite consensus disorder prediction
192 211 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
12 35 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
318 484 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
318 484 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
265 329 SMART SM00388 HisKA_10
264 328 Gene3D G3DSA:1.10.287.130 -
1 11 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
374 486 SMART SM00387 HKATPase_4
374 486 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
212 492 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
212 264 SMART SM00304 HAMP_11
212 264 InterPro IPR003660 HAMP domain
210 260 Pfam PF00672 HAMP domain
210 260 InterPro IPR003660 HAMP domain
36 192 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
213 261 SUPERFAMILY SSF158472 HAMP domain-like
272 486 ProSiteProfiles PS50109 Histidine kinase domain profile.
272 486 InterPro IPR005467 Histidine kinase domain
470 483 PRINTS PR00344 Bacterial sensor protein C-terminal signature
470 483 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
446 464 PRINTS PR00344 Bacterial sensor protein C-terminal signature
446 464 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
429 439 PRINTS PR00344 Bacterial sensor protein C-terminal signature
429 439 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
193 211 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
212 264 ProSiteProfiles PS50885 HAMP domain profile.
263 324 CDD cd00082 HisKA
263 324 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor 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_A0A0H3GSM3
AlphaFold — — full sequence — Viewing
ColabFold KP13_03152
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
26 0.371

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 14.73 0.732
2 3.51 0.129
3 3.46 0.125
4 2.48 0.069

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
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
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.