Overview
Basic information about this protein and its source genome.
- Accession
- KP13_31576
- Gene
- AHE43071.1
- Status
- annotated
- Amino acids
- 390
- 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 (%)
- 50.535
- DEG E-value
- 7.37e-125
- Localization
- CytoplasmicMembrane
- ColabFold pLDDT
- 91.78
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)
6- GO:1990961 A process that reduces or removes the toxicity of a xenobiotic by exporting it outside the cell.
- GO:0042910 Enables the directed movement of a xenobiotic from one side of a membrane to the other. A xenobiotic is a compound foreign to the organism exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
- GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
- 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:0015721 The directed movement of bile acid and bile salts into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
- GO:0046677 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 56 | 113 | SUPERFAMILY | SSF111369 | HlyD-like secretion proteins |
| 61 | 124 | Gene3D | G3DSA:2.40.50.100 | - |
| 23 | 44 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 36 | 345 | Pfam | PF00529 | Cation efflux system protein CusB domain 1 |
| 36 | 345 | InterPro | IPR043602 | Cation efflux system protein CusB, domain 1 |
| 160 | 180 | Coils | Coil | Coil |
| 1 | 361 | PANTHER | PTHR30386 | MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP |
| 194 | 270 | SUPERFAMILY | SSF111369 | HlyD-like secretion proteins |
| 234 | 354 | Gene3D | G3DSA:2.40.30.170 | - |
| 23 | 45 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 232 | 354 | FunFam | G3DSA:2.40.30.170:FF:000003 | Multidrug resistance protein A |
| 170 | 289 | Pfam | PF16576 | Barrel-sandwich domain of CusB or HlyD membrane-fusion |
| 170 | 289 | InterPro | IPR032317 | RND efflux pump, membrane fusion protein, barrel-sandwich domain |
| 20 | 345 | NCBIfam | TIGR00998 | EmrA/EmrK family multidrug efflux transporter periplasmic adaptor subunit |
| 20 | 345 | InterPro | IPR005694 | Membrane fusion proteins, proteobacteria |
| 45 | 390 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 122 | 142 | Coils | Coil | Coil |
| 1 | 22 | 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.
No pockets are loaded yet for the displayed AlphaFold model AF_A0A0H3GWJ4 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.
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_A0A0H3GWJ4
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_31576
|
ColabFold | — | — | full sequence | — | Loaded |