Protein profile
KP13_01848
Type 4 prepilin-like proteins leader peptide-processing enzyme bifunctional protein
Genome: KpKP13
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_01848
- Gene
- pulO AHE46288.1
- Status
- annotated
- Amino acids
- 266
- 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 (%)
- 49.434
- DEG E-value
- 1.02e-70
- Localization
- CytoplasmicMembrane
- ColabFold pLDDT
- 93.09
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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
- GO:0004190 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
- 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:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.
- GO:0032259 The process in which a methyl group is covalently attached to a molecule.
- GO:0006465 OBSOLETE. The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 245 | 262 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 132 | 149 | PRINTS | PR00864 | Type IV prepilin cysteine protease (C20) family signature |
| 132 | 149 | InterPro | IPR014032 | Peptidase A24A, prepilin type IV, bacterial |
| 200 | 211 | PRINTS | PR00864 | Type IV prepilin cysteine protease (C20) family signature |
| 200 | 211 | InterPro | IPR014032 | Peptidase A24A, prepilin type IV, bacterial |
| 189 | 199 | PRINTS | PR00864 | Type IV prepilin cysteine protease (C20) family signature |
| 189 | 199 | InterPro | IPR014032 | Peptidase A24A, prepilin type IV, bacterial |
| 212 | 227 | PRINTS | PR00864 | Type IV prepilin cysteine protease (C20) family signature |
| 212 | 227 | InterPro | IPR014032 | Peptidase A24A, prepilin type IV, bacterial |
| 13 | 35 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 123 | 231 | Pfam | PF01478 | Type IV leader peptidase family |
| 123 | 231 | InterPro | IPR000045 | Prepilin type IV endopeptidase, peptidase domain |
| 136 | 146 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 203 | 233 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 192 | 202 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 234 | 244 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 148 | 165 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 114 | 118 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 167 | 171 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 172 | 191 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 13 | 33 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 263 | 266 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 115 | 248 | Gene3D | G3DSA:1.20.120.1220 | - |
| 147 | 166 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 34 | 91 | Phobius | CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. |
| 169 | 191 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 1 | 12 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 13 | 265 | PANTHER | PTHR30487 | TYPE 4 PREPILIN-LIKE PROTEINS LEADER PEPTIDE-PROCESSING ENZYME |
| 240 | 262 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 91 | 113 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 21 | 109 | Pfam | PF06750 | Bacterial Peptidase A24 N-terminal domain |
| 21 | 109 | InterPro | IPR010627 | Peptidase A24A, N-terminal |
| 92 | 113 | Phobius | TRANSMEMBRANE | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 203 | 225 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 117 | 135 | TMHMM | TMhelix | Region of a membrane-bound protein predicted to be embedded in the membrane. |
| 119 | 135 | 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.
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_A0A0H3GRY2
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01848
|
ColabFold | — | — | full sequence | — | Loaded |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
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 | 10.23 | 0.55 | ||||||
| 2 | 4.21 | 0.171 | ||||||
| 3 | 4.12 | 0.166 | ||||||
| 4 | 1.94 | 0.04 | ||||||
| 5 | 1.84 | 0.036 |
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 | 0.818 |
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 | 3.64 | 0.136 | ||||||
| 3 | 2.37 | 0.062 | ||||||
| 4 | 2.25 | 0.056 | ||||||
| 5 | 2.08 | 0.047 |