Protein profile
VK055_4068
gram-negative pili assembly chaperone, C-terminal domain protein
Genome: KpATCC43816
Overview
Basic information about this protein and its source genome.
- Accession
- VK055_4068
- Gene
- AIK82615.1
- Status
- annotated
- Amino acids
- 243
- 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)
- N
- DEG identity (%)
- 32.759
- Localization
- Periplasmic
- ColabFold pLDDT
- 90.83
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)
4- GO:0043711 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pilus, a short filamentous structure on a bacterial cell, flagella-like in structure and generally present in many copies.
- GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
- GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
- GO:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 157 | 239 | Gene3D | G3DSA:2.60.40.10 | Immunoglobulins |
| 157 | 239 | InterPro | IPR013783 | Immunoglobulin-like fold |
| 24 | 243 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 5 | 236 | PANTHER | PTHR30251 | PILUS ASSEMBLY CHAPERONE |
| 176 | 235 | Pfam | PF02753 | Pili assembly chaperone PapD, C-terminal domain |
| 176 | 235 | InterPro | IPR016148 | Pili assembly chaperone, C-terminal |
| 7 | 26 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 136 | 151 | PRINTS | PR00969 | Pili chaperone signature |
| 136 | 151 | InterPro | IPR001829 | Pili assembly chaperone, bacterial |
| 171 | 186 | PRINTS | PR00969 | Pili chaperone signature |
| 171 | 186 | InterPro | IPR001829 | Pili assembly chaperone, bacterial |
| 75 | 96 | PRINTS | PR00969 | Pili chaperone signature |
| 75 | 96 | InterPro | IPR001829 | Pili assembly chaperone, bacterial |
| 25 | 34 | PRINTS | PR00969 | Pili chaperone signature |
| 25 | 34 | InterPro | IPR001829 | Pili assembly chaperone, bacterial |
| 105 | 122 | PRINTS | PR00969 | Pili chaperone signature |
| 105 | 122 | InterPro | IPR001829 | Pili assembly chaperone, bacterial |
| 1 | 23 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 24 | 154 | Pfam | PF00345 | Pili and flagellar-assembly chaperone, PapD N-terminal domain |
| 24 | 154 | InterPro | IPR016147 | Pili assembly chaperone, N-terminal |
| 19 | 23 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 25 | 151 | Gene3D | G3DSA:2.60.40.10 | Immunoglobulins |
| 25 | 151 | InterPro | IPR013783 | Immunoglobulin-like fold |
| 20 | 154 | SUPERFAMILY | SSF49354 | PapD-like |
| 20 | 154 | InterPro | IPR008962 | PapD-like superfamily |
| 1 | 21 | SignalP_EUK | SignalP-TM | SignalP-TM |
| 1 | 6 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 1 | 23 | SignalP_GRAM_NEGATIVE | SignalP-TM | SignalP-TM |
| 7 | 18 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 159 | 237 | SUPERFAMILY | SSF49584 | Periplasmic chaperone C-domain |
| 159 | 237 | InterPro | IPR036316 | Pili assembly chaperone, C-terminal 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.
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_A0A9Q6A0H3
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
VK055_4068
|
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 |
|---|---|---|---|---|---|---|---|
| 4 | 0.154 | ||||||
| 3 | 0.004 | ||||||
| 1 | 0.003 | ||||||
| 12 | 0.0 |
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 | 0.011 | ||||||
| 2 | 0.0 | ||||||
| 5 | 0.0 | ||||||
| 13 | 0.0 |
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 | 1.16 | 0.008 | ||||||
| 2 | 1.1 | 0.007 |
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 |
|---|---|---|---|---|---|---|
| EC2 | P15319 | 453.6 Da LogP 5.94 TPSA 59.3 | 1 viol. | ✓ Clean |
c1ccc(cc1)[C@@H]2[C@H](N3C(=O)C=C(C(=C3S2)C4CC4…
|
|
| EC5 | P15319 | 471.6 Da LogP 5.90 TPSA 79.5 | 1 viol. | ✓ Clean |
c1ccc(cc1)C[C@@H](C(=O)O)N2C(=O)C=C(C(=C2SO)C3C…
|
|
| XC2 | P15319 | 476.6 Da LogP 4.03 TPSA 71.8 | ✓ Ro5 | ✓ Clean |
c1ccc2c(c1)cccc2CC3=C(C(=O)N4[C@@H](CSC4=C3C5CC…
|
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.