Protein profile
KP13_01037
Penicillin-insensitive murein endopeptidase
Genome: KpKP13
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_01037
- Gene
- AHE43435.1 mepA
- Status
- annotated
- Amino acids
- 274
- 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
- Periplasmic
- ColabFold pLDDT
- 93.27
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)
6- GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
- GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
- GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
- GO:0046872 Binding to a metal ion.
- 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:0000270 The chemical reactions and pathways involving peptidoglycans, any of a class of glycoconjugates found only in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 246 | 265 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 224 | 274 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 4 | 14 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 3 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 1 | 274 | PIRSF | PIRSF018455 | MepA |
| 1 | 274 | InterPro | IPR005073 | Peptidase M74, penicillin-insensitive murein endopeptidase |
| 21 | 272 | SUPERFAMILY | SSF55166 | Hedgehog/DD-peptidase |
| 21 | 272 | InterPro | IPR009045 | Hedgehog signalling/DD-peptidase zinc-binding domain superfamily |
| 36 | 270 | Pfam | PF03411 | Penicillin-insensitive murein endopeptidase |
| 36 | 270 | InterPro | IPR005073 | Peptidase M74, penicillin-insensitive murein endopeptidase |
| 20 | 274 | Gene3D | G3DSA:3.30.1380.10 | - |
| 20 | 274 | InterPro | IPR009045 | Hedgehog signalling/DD-peptidase zinc-binding domain superfamily |
| 20 | 274 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 1 | 19 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 1 | 19 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 15 | 19 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 1 | 274 | Hamap | MF_01623 | Penicillin-insensitive murein endopeptidase [mepA]. |
| 1 | 19 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
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_A0A0H3GR96
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01037
|
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 |
|---|---|---|---|---|---|---|---|
| 1 | 0.248 |
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 | 15.81 | 0.763 |
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 | 0.293 |
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 | 8.37 | 0.446 | ||||||
| 2 | 7.43 | 0.39 | ||||||
| 3 | 1.35 | 0.016 |