Protein profile

KP13_03033

Sensor protein BasS

Genome: KpKP13

Gene: AHE45581.1 basS Structure source: AlphaFold + ColabFold UniProt A0A0H3GQH3
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Amino acids 365
Annotations 7
Features 37
PDB binders 3
Druggability 0.123

Overview

Basic information about this protein and its source genome.

Accession
KP13_03033
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45581.1 basS
Status
annotated
Amino acids
365
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
78.55

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 0.123
Structure A0A0H3GQH3
Pocket Pocket 8
P2Rank 0.599
Structure A0A0H3GQH3
Pocket Pocket 1
ColabFold model
FPocket 0.916 · Pocket 14
P2Rank 0.862 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 72 / 4744 genomes with a hit
Normalized 0.015

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.

37 records
Show feature table
Start End DB Term Name
52 143 Gene3D G3DSA:6.10.340.10 -
141 199 CDD cd00082 HisKA
141 199 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
144 202 Gene3D G3DSA:1.10.287.130 -
13 35 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
90 142 SMART SM00304 HAMP_11
90 142 InterPro IPR003660 HAMP domain
66 89 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
1 14 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
250 355 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
250 355 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
90 142 ProSiteProfiles PS50885 HAMP domain profile.
250 358 SMART SM00387 HKATPase_4
250 358 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
145 201 Pfam PF00512 His Kinase A (phospho-acceptor) domain
145 201 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
15 35 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
90 365 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
67 89 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
215 355 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
215 355 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
56 357 PANTHER PTHR45436 SENSOR HISTIDINE KINASE YKOH
143 203 SMART SM00388 HisKA_10
143 203 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
210 357 Gene3D G3DSA:3.30.565.10 -
210 357 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
286 300 PRINTS PR00344 Bacterial sensor protein C-terminal signature
286 300 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
342 355 PRINTS PR00344 Bacterial sensor protein C-terminal signature
342 355 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
317 335 PRINTS PR00344 Bacterial sensor protein C-terminal signature
317 335 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
36 65 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
150 358 ProSiteProfiles PS50109 Histidine kinase domain profile.
150 358 InterPro IPR005467 Histidine kinase domain
127 201 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
127 201 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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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_A0A0H3GQH3
AlphaFold — — full sequence — Viewing
ColabFold KP13_03033
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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 8.17 0.435

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.