Overview
Basic information about this protein and its source genome.
- Accession
- PA0572
- Gene
- PA0572 impA
- Status
- annotated
- Amino acids
- 923
- 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
- OuterMembrane
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.
Enzyme Commission (EC)
1Gene Ontology (GO)
8- GO:0005615 OBSOLETE. That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
- GO:0046872 Binding to a metal ion.
- GO:0008237 Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
- GO:1903237 Any process that stops, prevents or reduces the frequency, rate or extent of leukocyte tethering or rolling.
- GO:0030163 The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
- GO:0015628 The process in which proteins are secreted across the outer membrane of Gram-negative bacteria by the type II secretion system. Proteins using this pathway are first translocated across the cytoplasmic membrane via the Sec or Tat pathways.
- GO:0043952 The process in which unfolded proteins are transported across the cytoplasmic membrane in Gram-positive and Gram-negative bacteria by the Sec complex, in a process involving proteolytic cleavage of an N-terminal signal peptide.
- GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 84 | 278 | Pfam | PF18650 | Immunomodulating metalloprotease N-terminal domain |
| 84 | 278 | InterPro | IPR040711 | Immunomodulating metalloprotease N-terminal domain |
| 562 | 873 | Pfam | PF13402 | Peptidase M60, enhancin and enhancin-like |
| 562 | 873 | InterPro | IPR031161 | Peptidase family M60 domain |
| 38 | 41 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 42 | 923 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 710 | 909 | Gene3D | G3DSA:1.10.390.30 | - |
| 710 | 909 | InterPro | IPR042279 | Peptidase M60, enhancin-like domain 3 |
| 450 | 794 | ProSiteProfiles | PS51723 | Peptidase family M60 domain profile. |
| 450 | 794 | InterPro | IPR031161 | Peptidase family M60 domain |
| 1 | 25 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 26 | 37 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 41 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 305 | 414 | Pfam | PF18642 | Immunomodulating metalloprotease helical domain |
| 305 | 414 | InterPro | IPR041549 | Immunomodulating metalloprotease helical domain |
| 450 | 795 | SMART | SM01276 | M60_like_2 |
| 450 | 795 | InterPro | IPR031161 | Peptidase family M60 domain |
| 1 | 41 | SignalP_GRAM_NEGATIVE | SignalP-noTM | SignalP-noTM |
| 51 | 920 | NCBIfam | NF038322 | ImpA family metalloprotease |
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
4 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
PDB
5KDW
|
X-ray | 1.85 Å | A,B |
|
Viewing | |
|
PDB
5KDV
|
X-ray | 1.93 Å | A |
|
Loaded | |
|
PDB
5KDX
|
X-ray | 2.40 Å | A,B |
|
Loaded | |
|
PDB
7JTV
|
X-ray | 2.45 Å | A,B |
|
Loaded | |
|
AlphaFold
PA0572
|
AlphaFold | — | — | full sequence | — | Loaded |
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.819 | ||||||
| 9 | 0.495 | ||||||
| 2 | 0.466 |
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 | 11.15 | 0.598 | ||||||
| 2 | 10.49 | 0.564 | ||||||
| 3 | 7.99 | 0.425 | ||||||
| 4 | 6.87 | 0.353 | ||||||
| 5 | 5.31 | 0.25 |
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.648 |