Protein profile

PA1692

translocation protein in type III secretion

Genome: NC_002516.2

Gene: PA1692 Structure source: AlphaFold UniProt Q9I335
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Amino acids 88
Annotations 4
Features 21
PDB binders 2
Druggability 0.801

Overview

Basic information about this protein and its source genome.

Accession
PA1692
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1692
Status
annotated
Amino acids
88
Structure source
AlphaFold
GO
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:0044780 The assembly of a bacterial-type flagellum, a motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope which functions in cell motility. GO:0009306 The controlled release of proteins from a cell. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
Y
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.

FPocket 0.801
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • 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:0044780 The assembly of a bacterial-type flagellum, a motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope which functions in cell motility.
  • GO:0009306 The controlled release of proteins from a 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.

21 records
Show feature table
Start End DB Term Name
49 69 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
15 37 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
5 84 NCBIfam TIGR01403 type III secretion system export apparatus subunit SctS
5 84 InterPro IPR006306 Type III secretion protein HrpO
49 71 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
39 54 PRINTS PR00952 Type III secretion system inner membrane Q protein family signature
39 54 InterPro IPR002191 Bacterial export protein family 3
54 76 PRINTS PR00952 Type III secretion system inner membrane Q protein family signature
54 76 InterPro IPR002191 Bacterial export protein family 3
18 39 PRINTS PR00952 Type III secretion system inner membrane Q protein family signature
18 39 InterPro IPR002191 Bacterial export protein family 3
1 88 PIRSF PIRSF004669 FliQ
1 88 InterPro IPR002191 Bacterial export protein family 3
70 88 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 87 PANTHER PTHR34040 FLAGELLAR BIOSYNTHETIC PROTEIN FLIQ
1 87 InterPro IPR002191 Bacterial export protein family 3
38 48 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
6 77 Pfam PF01313 Bacterial export proteins, family 3
6 77 InterPro IPR002191 Bacterial export protein family 3
1 11 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
12 37 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA1692
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
2 0.801
1 0.582

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.

52 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
3PH
7AH9
P0A1L7 705.0 Da LogP 12.07 TPSA 119.4 2 viol. ✓ Clean CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O…
LDA
7AH9
P0A1L7 229.4 Da LogP 4.48 TPSA 23.1 ✓ Ro5 ✓ Clean CCCCCCCCCCCC[N+](C)(C)[O-]

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.