Protein target profile
PA1102
flagellar motor switch protein FliG
Genome: NC_002516.2
Target candidate with partial support; inspect missing evidence before prioritizing.
4 signalsStrengths
Risks / watch
How to read this page
PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.
AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.
ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.
pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.
FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.
Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.
PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.
ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.
ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.
LigQ / LigQ_2: an internal TPW pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.
Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.
DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.
Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.
EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.
KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.
Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.
Overview
Basic information about this protein and its source genome.
- Accession
- PA1102
- Gene
- PA1102 fliG
- Status
- annotated
- Amino acids
- 338
- 3D evidence
- AlphaFold DB model
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- Localization
- Cytoplasmic
Selected pocket evidence
The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
MSENRLAAKLTKVDKAAILLLSLGETDAAQVLRHMGPKEVQRVGVAMASMRNVHREQVEQVMGEFVEVVGDQTSLGVGADGYIRKMLTQALGEDKANNLIDRILLGGSTSGLDSLKWMEPRAVADVIRYEHPQIQAIVVAYLDPDQAAEVLSHFDHKVRLDIVLRVSSLNTVQPSALKELNLILEKQFAGNSNATRTTMGGVKRAADIMNYLDSSIEGQLMDSIREVDEDLSGQIEDLMFVFDNLADVDDRGIQALLREVSSDVLVLALKGSDEAIREKVFKNMSKRAAELLRDDLEAKGPVRVSEVEGAQKEILTIARRMAESGDIVLGGKGGEEMI
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
6- GO:0009425 One of the three major substructures of the bacterial-type flagellum, the basal body is embedded in the cell envelope (the plasma membrane, peptidoglycan cell wall, and, if one is present, the outer membrane); it houses the secretion apparatus that exports the more distal components and the flagellar motor.
- 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:0003774 Generation of force resulting in movement, for example along a microfilament or microtubule, or in torque resulting in membrane scission or rotation of a flagellum. The energy required is obtained either from the hydrolysis of a nucleoside triphosphate or by an electrochemical proton gradient (proton-motive force).
- GO:0071973 Cell motility due to the motion of one or more bacterial-type flagella. A bacterial-type flagellum is a motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope.
- 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:0009288 A motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 200 | 225 | PRINTS | PR00954 | Flagellar motor switch protein FliG signature |
| 200 | 225 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 39 | 65 | PRINTS | PR00954 | Flagellar motor switch protein FliG signature |
| 39 | 65 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 231 | 251 | PRINTS | PR00954 | Flagellar motor switch protein FliG signature |
| 231 | 251 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 253 | 273 | PRINTS | PR00954 | Flagellar motor switch protein FliG signature |
| 253 | 273 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 10 | 26 | PRINTS | PR00954 | Flagellar motor switch protein FliG signature |
| 10 | 26 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 277 | 303 | PRINTS | PR00954 | Flagellar motor switch protein FliG signature |
| 277 | 303 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 119 | 142 | PRINTS | PR00954 | Flagellar motor switch protein FliG signature |
| 119 | 142 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 93 | 194 | Gene3D | G3DSA:1.10.220.30 | - |
| 12 | 122 | SUPERFAMILY | SSF48029 | FliG |
| 12 | 122 | InterPro | IPR011002 | Flagellar motor switch protein FliG, alpha-helical |
| 119 | 330 | SUPERFAMILY | SSF48029 | FliG |
| 119 | 330 | InterPro | IPR011002 | Flagellar motor switch protein FliG, alpha-helical |
| 24 | 28 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 200 | 338 | Gene3D | G3DSA:1.10.220.30 | - |
| 3 | 337 | PANTHER | PTHR30534 | FLAGELLAR MOTOR SWITCH PROTEIN FLIG |
| 3 | 337 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 16 | 23 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 5 | 338 | PIRSF | PIRSF003161 | FliG |
| 5 | 338 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 1 | 15 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 223 | 329 | Pfam | PF01706 | FliG C-terminal domain |
| 223 | 329 | InterPro | IPR023087 | Flagellar motor switch protein FliG, C-terminal |
| 120 | 193 | Pfam | PF14841 | FliG middle domain |
| 120 | 193 | InterPro | IPR032779 | Flagellar motor switch protein FliG, middle domain |
| 7 | 336 | NCBIfam | TIGR00207 | flagellar motor switch protein FliG |
| 7 | 336 | InterPro | IPR000090 | Flagellar motor switch protein FliG |
| 6 | 90 | FunFam | G3DSA:1.10.220.30:FF:000007 | Flagellar motor switch protein FliG |
| 29 | 338 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 1 | 28 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 4 | 90 | Gene3D | G3DSA:1.10.220.30 | - |
| 200 | 338 | FunFam | G3DSA:1.10.220.30:FF:000001 | Flagellar motor switch protein FliG |
| 94 | 196 | FunFam | G3DSA:1.10.220.30:FF:000004 | Flagellar motor switch protein FliG |
| 9 | 108 | Pfam | PF14842 | FliG N-terminal domain |
| 9 | 108 | InterPro | IPR028263 | Flagellar motor switch protein FliG, N-terminal domain |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold DB
PA1102
|
AlphaFold DB | — | — | 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 | Sector atoms | Sector | Druggability | Labels | Zoom | Positions | |
|---|---|---|---|---|---|---|---|
| 1 | 0.418 | ||||||
| 6 | 0.306 | ||||||
| 2 | 0.202 |