Overview
Basic information about this protein and its source genome.
- Accession
- PA4924
- Gene
- PA4924
- Status
- annotated
- Amino acids
- 231
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- 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.
Gene Ontology (GO)
4- GO:0032153 The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
- GO:0009279 A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures.
- 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: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.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 131 | 215 | CDD | cd12797 | M23_peptidase |
| 94 | 226 | PANTHER | PTHR21666 | PEPTIDASE-RELATED |
| 20 | 231 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 34 | 78 | ProSiteProfiles | PS51782 | LysM domain profile. |
| 34 | 78 | InterPro | IPR018392 | LysM domain |
| 1 | 21 | SignalP_GRAM_NEGATIVE | SignalP-noTM | SignalP-noTM |
| 1 | 19 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 1 | 19 | SignalP_EUK | SignalP-noTM | SignalP-noTM |
| 34 | 74 | FunFam | G3DSA:3.10.350.10:FF:000006 | YgeR family lipoprotein |
| 77 | 229 | Gene3D | G3DSA:2.70.70.10 | Glucose Permease (Domain IIA) |
| 77 | 229 | InterPro | IPR011055 | Duplicated hybrid motif |
| 87 | 106 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 36 | 77 | CDD | cd00118 | LysM |
| 36 | 77 | InterPro | IPR018392 | LysM domain |
| 36 | 76 | Pfam | PF01476 | LysM domain |
| 36 | 76 | InterPro | IPR018392 | LysM domain |
| 87 | 229 | FunFam | G3DSA:2.70.70.10:FF:000010 | M23 family peptidase |
| 131 | 224 | Pfam | PF01551 | Peptidase family M23 |
| 131 | 224 | InterPro | IPR016047 | Peptidase M23 |
| 35 | 76 | Gene3D | G3DSA:3.10.350.10 | LysM domain |
| 35 | 76 | InterPro | IPR036779 | LysM domain superfamily |
| 35 | 79 | SMART | SM00257 | LysM_2 |
| 35 | 79 | InterPro | IPR018392 | LysM domain |
| 1 | 21 | SignalP_GRAM_POSITIVE | SignalP-TM | SignalP-TM |
| 1 | 4 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 5 | 14 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 1 | 17 | ProSiteProfiles | PS51257 | Prokaryotic membrane lipoprotein lipid attachment site profile. |
| 36 | 228 | SUPERFAMILY | SSF51261 | Duplicated hybrid motif |
| 36 | 228 | InterPro | IPR011055 | Duplicated hybrid motif |
| 15 | 19 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
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 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA4924
|
AlphaFold | — | — | full sequence | — | Viewing |
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 | 0.954 |