Overview
Basic information about this protein and its source genome.
- Accession
- PA2652
- Gene
- ctpM PA2652
- Status
- annotated
- Amino acids
- 561
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 21.254
- Human E-value
- 6.16e-07
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- CytoplasmicMembrane
Selected Druggability evidence
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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
6- 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:0004888 Combining with an extracellular or intracellular signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity or state as part of signal transduction.
- GO:0006935 The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
- GO:0050918 The directed movement of a motile cell or organism towards a higher concentration of a chemical.
- 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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 333 | 356 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 1 | 39 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 30 | 206 | Gene3D | G3DSA:3.30.450.20 | PAS domain |
| 10 | 21 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 10 | 32 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 230 | 284 | ProSiteProfiles | PS50885 | HAMP domain profile. |
| 230 | 284 | InterPro | IPR003660 | HAMP domain |
| 45 | 136 | SMART | SM01049 | Cache_2_2 |
| 45 | 136 | InterPro | IPR033480 | Single Cache domain 2 |
| 233 | 279 | CDD | cd06225 | HAMP |
| 22 | 26 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 230 | 561 | FunFam | G3DSA:1.10.287.950:FF:000001 | Methyl-accepting chemotaxis sensory transducer |
| 293 | 317 | Coils | Coil | Coil |
| 344 | 526 | Pfam | PF00015 | Methyl-accepting chemotaxis protein (MCP) signalling domain |
| 344 | 526 | InterPro | IPR004089 | Methyl-accepting chemotaxis protein (MCP) signalling domain |
| 289 | 525 | ProSiteProfiles | PS50111 | Bacterial chemotaxis sensory transducers domain profile. |
| 289 | 525 | InterPro | IPR004089 | Methyl-accepting chemotaxis protein (MCP) signalling domain |
| 299 | 560 | SMART | SM00283 | MA_2 |
| 299 | 560 | InterPro | IPR004089 | Methyl-accepting chemotaxis protein (MCP) signalling domain |
| 27 | 205 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 15 | 560 | PANTHER | PTHR32089 | METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB |
| 230 | 284 | SMART | SM00304 | HAMP_11 |
| 326 | 525 | CDD | cd11386 | MCP_signal |
| 426 | 455 | PRINTS | PR00260 | Bacterial chemotaxis sensory transducer signature |
| 426 | 455 | InterPro | IPR004090 | Chemotaxis methyl-accepting receptor |
| 397 | 424 | PRINTS | PR00260 | Bacterial chemotaxis sensory transducer signature |
| 397 | 424 | InterPro | IPR004090 | Chemotaxis methyl-accepting receptor |
| 6 | 31 | PRINTS | PR00260 | Bacterial chemotaxis sensory transducer signature |
| 6 | 31 | InterPro | IPR004090 | Chemotaxis methyl-accepting receptor |
| 320 | 349 | PRINTS | PR00260 | Bacterial chemotaxis sensory transducer signature |
| 320 | 349 | InterPro | IPR004090 | Chemotaxis methyl-accepting receptor |
| 234 | 561 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 1 | 26 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 206 | 233 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 228 | 280 | Pfam | PF00672 | HAMP domain |
| 228 | 280 | InterPro | IPR003660 | HAMP domain |
| 252 | 561 | SUPERFAMILY | SSF58104 | Methyl-accepting chemotaxis protein (MCP) signaling domain |
| 51 | 196 | Pfam | PF17200 | Single Cache domain 2 |
| 51 | 196 | InterPro | IPR033480 | Single Cache domain 2 |
| 206 | 228 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 476 | 538 | ProSiteProfiles | PS50192 | t-SNARE coiled-coil homology domain profile. |
| 476 | 538 | InterPro | IPR000727 | Target SNARE coiled-coil homology domain |
| 230 | 561 | Gene3D | G3DSA:1.10.287.950 | - |
| 1 | 9 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 489 | 509 | Coils | Coil | Coil |
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 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA2652
|
AlphaFold | — | — | full sequence | — | Viewing |
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 |
|---|---|---|---|---|---|---|---|
| 7 | 0.82 | ||||||
| 2 | 0.656 | ||||||
| 4 | 0.338 | ||||||
| 3 | 0.261 |
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 |
|---|---|---|---|---|---|---|
| ACM | B6JPK4 | 59.1 Da LogP -0.51 TPSA 43.1 | ✓ Ro5 | ✓ Clean |
CC(=O)N
|
|
| ARF | B6JPK4 | 45.0 Da LogP -0.90 TPSA 43.1 | ✓ Ro5 | ✓ Clean |
C(=O)N
|
|
| NHY | B6JPK4 | 76.1 Da LogP -0.96 TPSA 75.4 | ✓ Ro5 | ✓ Clean |
C(=O)(N)NO
|
|
| PYR | Q87T87 | 88.1 Da LogP -0.34 TPSA 54.4 | ✓ Ro5 | ✓ Clean |
CC(=O)C(=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.