Overview
Basic information about this protein and its source genome.
- Accession
- KP13_03820
- Gene
- AHE43304.1
- Status
- annotated
- Amino acids
- 487
- 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)
- N
- DEG identity (%)
- 0.0
- Localization
- Unknown
- ColabFold pLDDT
- 88.26
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.
Enzyme Commission (EC)
1Gene Ontology (GO)
9- GO:0004222 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain 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:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
- GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
- GO:0005515 Binding to a protein.
- 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:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
- GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
- GO:0008270 Binding to a zinc ion (Zn).
- GO:0051603 OBSOLETE. The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 313 | 428 | SUPERFAMILY | SSF48452 | TPR-like |
| 313 | 428 | InterPro | IPR011990 | Tetratricopeptide-like helical domain superfamily |
| 4 | 484 | Hamap | MF_00997 | Beta-barrel assembly-enhancing protease [bepA]. |
| 4 | 484 | InterPro | IPR030873 | Beta-barrel assembly-enhancing protease |
| 1 | 7 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 75 | 150 | Gene3D | G3DSA:3.30.2010.10 | Metalloproteases ("zincins"), catalytic domain |
| 354 | 418 | Pfam | PF14559 | Tetratricopeptide repeat |
| 79 | 259 | Pfam | PF01435 | Peptidase family M48 |
| 79 | 259 | InterPro | IPR001915 | Peptidase M48 |
| 48 | 262 | CDD | cd07333 | M48C_bepA_like |
| 28 | 487 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 1 | 27 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 269 | 483 | Gene3D | G3DSA:1.25.40.10 | Tetratricopeptide repeat domain |
| 269 | 483 | InterPro | IPR011990 | Tetratricopeptide-like helical domain superfamily |
| 1 | 27 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 20 | 27 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 5 | 265 | PANTHER | PTHR22726 | METALLOENDOPEPTIDASE OMA1 |
| 8 | 19 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 27 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
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
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_A0A0H3GW14
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_03820
|
ColabFold | — | — | 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 |
|---|---|---|---|---|---|---|---|
| 31 | 0.818 | ||||||
| 3 | 0.652 | ||||||
| 1 | 0.203 |
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 | 5.23 | 0.243 | ||||||
| 2 | 4.37 | 0.183 | ||||||
| 3 | 3.89 | 0.153 | ||||||
| 4 | 3.33 | 0.118 | ||||||
| 5 | 2.83 | 0.088 |
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 |
|---|---|---|---|---|---|---|---|
| 30 | 0.725 |
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 | 5.06 | 0.231 | ||||||
| 2 | 4.62 | 0.2 | ||||||
| 3 | 3.22 | 0.111 | ||||||
| 4 | 2.83 | 0.088 | ||||||
| 5 | 1.9 | 0.038 |