Overview
Basic information about this protein and its source genome.
- Accession
- KP13_01590
- Gene
- prc AHE43885.1
- Status
- annotated
- Amino acids
- 682
- 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 (%)
- 90.909
- DEG E-value
- 0.0
- Localization
- CytoplasmicMembrane
- ColabFold pLDDT
- 92.66
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.
Enzyme Commission (EC)
1Gene Ontology (GO)
7- GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
- GO:0005515 Binding to a protein.
- GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
- 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:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
- GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
- 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.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 341 | 528 | Gene3D | G3DSA:3.90.226.10 | - |
| 1 | 6 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 194 | 551 | NCBIfam | TIGR00225 | C-terminal processing peptidase |
| 194 | 551 | InterPro | IPR004447 | C-terminal-processing peptidase S41A |
| 633 | 656 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 536 | 667 | Pfam | PF11818 | C-terminal domain of tail specific protease (DUF3340) |
| 536 | 667 | InterPro | IPR020992 | Tail specific protease, C-terminal |
| 238 | 308 | ProSiteProfiles | PS50106 | PDZ domain profile. |
| 238 | 308 | InterPro | IPR001478 | PDZ domain |
| 246 | 340 | Gene3D | G3DSA:2.30.42.10 | - |
| 246 | 340 | InterPro | IPR036034 | PDZ superfamily |
| 246 | 340 | FunFam | G3DSA:2.30.42.10:FF:000083 | Tail-specific protease |
| 245 | 337 | CDD | cd00988 | PDZ_CTP_protease |
| 23 | 682 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 1 | 22 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 49 | 232 | Pfam | PF17804 | Tail specific protease N-terminal domain |
| 49 | 232 | InterPro | IPR040573 | Tail specific protease, N-terminal domain |
| 341 | 493 | FunFam | G3DSA:3.90.226.10:FF:000015 | Periplasmic tail-specific protease |
| 219 | 343 | SUPERFAMILY | SSF50156 | PDZ domain-like |
| 219 | 343 | InterPro | IPR036034 | PDZ superfamily |
| 633 | 655 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 194 | 538 | SUPERFAMILY | SSF52096 | ClpP/crotonase |
| 194 | 538 | InterPro | IPR029045 | ClpP/crotonase-like domain superfamily |
| 181 | 506 | Gene3D | G3DSA:3.30.750.44 | - |
| 614 | 634 | Coils | Coil | Coil |
| 356 | 531 | CDD | cd07560 | Peptidase_S41_CPP |
| 356 | 531 | InterPro | IPR004447 | C-terminal-processing peptidase S41A |
| 246 | 323 | SMART | SM00228 | pdz_new |
| 246 | 323 | InterPro | IPR001478 | PDZ domain |
| 240 | 320 | Pfam | PF00595 | PDZ domain |
| 240 | 320 | InterPro | IPR001478 | PDZ domain |
| 18 | 22 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 152 | 556 | PANTHER | PTHR32060 | TAIL-SPECIFIC PROTEASE |
| 356 | 528 | Pfam | PF03572 | Peptidase family S41 |
| 356 | 528 | InterPro | IPR005151 | Tail specific protease |
| 7 | 17 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 22 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 1 | 22 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 326 | 531 | SMART | SM00245 | tsp_4 |
| 326 | 531 | InterPro | IPR005151 | Tail specific protease |
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_A0A0H3GQ33
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01590
|
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 | 7.14 | 0.371 | ||||||
| 2 | 2.74 | 0.083 | ||||||
| 3 | 1.2 | 0.011 |
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 |
|---|---|---|---|---|---|---|---|
| 23 | 0.362 | ||||||
| 3 | 0.282 |
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 | 8.36 | 0.445 | ||||||
| 2 | 1.84 | 0.036 | ||||||
| 3 | 1.58 | 0.024 | ||||||
| 4 | 1.02 | 0.006 |
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 |
|---|---|---|---|---|---|---|
| TMO | A0A1E3M7A1 | 75.1 Da LogP 0.19 TPSA 23.1 | ✓ Ro5 | ✓ Clean |
C[N+](C)(C)[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.