Protein profile
KP13_05062
Alkaline phosphatase synthesis transcriptional regulatory protein phoP
Genome: KpKP13
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_05062
- Gene
- AHE44188.1
- Status
- annotated
- Amino acids
- 245
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 41.558
- DEG E-value
- 2.7e-42
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 85.04
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
7- GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
- GO:0000160 A conserved series of molecular signals found in prokaryotes and eukaryotes; involves autophosphorylation of a histidine kinase and the transfer of the phosphate group to an aspartate that then acts as a phospho-donor to response regulator proteins.
- GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
- GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
- GO:0032993 A macromolecular complex containing both protein and DNA molecules.
- GO:0000156 Responds to a phosphorelay sensor to initiate a change in cell state or activity. The activity of the response regulator is regulated by transfer of a phosphate from a histidine residue in the sensor, to an aspartate residue in the response regulator. Many but not all response regulators act as transcriptional regulators to elicit a response.
- GO:0000976 Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 172 | 241 | Pfam | PF00486 | Transcriptional regulatory protein, C terminal |
| 172 | 241 | InterPro | IPR001867 | OmpR/PhoB-type DNA-binding domain |
| 170 | 241 | SUPERFAMILY | SSF46894 | C-terminal effector domain of the bipartite response regulators |
| 170 | 241 | InterPro | IPR016032 | Signal transduction response regulator, C-terminal effector |
| 16 | 126 | SMART | SM00448 | REC_2 |
| 16 | 126 | InterPro | IPR001789 | Signal transduction response regulator, receiver domain |
| 148 | 245 | Gene3D | G3DSA:1.10.10.10 | - |
| 148 | 245 | InterPro | IPR036388 | Winged helix-like DNA-binding domain superfamily |
| 18 | 242 | PANTHER | PTHR48111 | REGULATOR OF RPOS |
| 18 | 242 | InterPro | IPR039420 | Transcriptional regulatory protein WalR-like |
| 18 | 126 | Pfam | PF00072 | Response regulator receiver domain |
| 18 | 126 | InterPro | IPR001789 | Signal transduction response regulator, receiver domain |
| 17 | 130 | ProSiteProfiles | PS50110 | Response regulatory domain profile. |
| 17 | 130 | InterPro | IPR001789 | Signal transduction response regulator, receiver domain |
| 168 | 241 | SMART | SM00862 | Trans_reg_C_3 |
| 168 | 241 | InterPro | IPR001867 | OmpR/PhoB-type DNA-binding domain |
| 142 | 243 | ProSiteProfiles | PS51755 | OmpR/PhoB-type DNA-binding domain profile. |
| 142 | 243 | InterPro | IPR001867 | OmpR/PhoB-type DNA-binding domain |
| 11 | 141 | SUPERFAMILY | SSF52172 | CheY-like |
| 11 | 141 | InterPro | IPR011006 | CheY-like superfamily |
| 172 | 241 | CDD | cd00383 | trans_reg_C |
| 100 | 132 | Gene3D | G3DSA:6.10.250.690 | - |
| 17 | 99 | Gene3D | G3DSA:3.40.50.2300 | - |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GZ70
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_05062
|
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 |
|---|---|---|---|---|---|---|---|
| 11 | 0.152 | ||||||
| 1 | 0.008 | ||||||
| 16 | 0.006 | ||||||
| 10 | 0.001 |
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 | 1.36 | 0.013 | ||||||
| 2 | 1.35 | 0.013 |
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 | 0.478 | ||||||
| 2 | 0.008 | ||||||
| 14 | 0.0 | ||||||
| 22 | 0.0 |
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.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
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.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| BEF | A0A0H2UQ68 | 66.0 Da LogP 0.88 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
[Be-](F)(F)F
|
|
| CAC | P71814 | 137.0 Da LogP -0.52 TPSA 40.1 | ✓ Ro5 | ✓ Clean |
C[As](=O)(C)[O-]
|
|
| PHS | A0A0H2UQ68 | 82.0 Da LogP -0.64 TPSA 57.5 | ✓ Ro5 | ✓ Clean |
OP(=O)O
|
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
No virtual-screening candidates for this protein.
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.