Overview
Basic information about this protein and its source genome.
- Accession
- PA0172
- Gene
- PA0172
- Status
- annotated
- Amino acids
- 663
- Structure source
- Experimental + AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- Unknown
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)
4- GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
- GO:0046872 Binding to a metal ion.
- GO:0016791 Catalysis of the hydrolysis of a phosphoric monoester, releasing a phosphate.
- 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 |
|---|---|---|---|---|
| 337 | 389 | SMART | SM00304 | HAMP_11 |
| 337 | 389 | InterPro | IPR003660 | HAMP domain |
| 384 | 415 | Coils | Coil | Coil |
| 6 | 663 | NCBIfam | NF038263 | biofilm regulation protein phosphatase SiaA |
| 337 | 386 | SUPERFAMILY | SSF158472 | HAMP domain-like |
| 466 | 663 | Pfam | PF07228 | Stage II sporulation protein E (SpoIIE) |
| 466 | 663 | InterPro | IPR001932 | PPM-type phosphatase-like domain |
| 304 | 396 | Gene3D | G3DSA:6.10.340.10 | - |
| 337 | 386 | Pfam | PF00672 | HAMP domain |
| 337 | 386 | InterPro | IPR003660 | HAMP domain |
| 404 | 661 | Gene3D | G3DSA:3.60.40.10 | - |
| 404 | 661 | InterPro | IPR036457 | PPM-type phosphatase-like domain superfamily |
| 312 | 335 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 192 | 301 | CDD | cd18774 | PDC2_HK_sensor |
| 312 | 334 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 24 | 30 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 1 | 11 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 12 | 31 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 337 | 389 | ProSiteProfiles | PS50885 | HAMP domain profile. |
| 44 | 663 | PANTHER | PTHR43156 | STAGE II SPORULATION PROTEIN E-RELATED |
| 1 | 30 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 453 | 662 | SMART | SM00331 | PP2C_SIG_2 |
| 453 | 662 | InterPro | IPR001932 | PPM-type phosphatase-like domain |
| 31 | 311 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 12 | 23 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 448 | 659 | SUPERFAMILY | SSF81606 | PP2C-like |
| 448 | 659 | InterPro | IPR036457 | PPM-type phosphatase-like domain superfamily |
| 350 | 383 | CDD | cd06225 | HAMP |
| 336 | 663 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
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
1 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
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 | 0.852 | ||||||
| 7 | 0.738 | ||||||
| 11 | 0.464 |
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 | 4.66 | 0.203 | ||||||
| 2 | 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 |
|---|---|---|---|---|---|---|---|
| 2 | 0.893 | ||||||
| 17 | 0.391 |