Protein profile
KP13_01546
Endo-type membrane-bound lytic murein transglycosylase A
Genome: KpKP13
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_01546
- Gene
- emtA AHE43925.1
- Status
- annotated
- Amino acids
- 167
- 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
- 97.2
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)
5- GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
- 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.
- GO:0008933 Catalysis of the cleavage of a peptidoglycan chain into a peptidoglycan chain with N-acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a peptidoglycan chain with N-acetylglucosamine at the non-reducing end. Includes endolytic transglycosylase activity that fragments the glycan chain internally and exolytic transgylcosylase activity that cleaves a terminal disaccharide from the end of the glycan strand.
- GO:0016798 Catalysis of the hydrolysis of any glycosyl bond.
- GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 162 | SUPERFAMILY | SSF53955 | Lysozyme-like |
| 1 | 162 | InterPro | IPR023346 | Lysozyme-like domain superfamily |
| 5 | 163 | CDD | cd16893 | LT_MltC_MltE |
| 1 | 167 | Gene3D | G3DSA:1.10.530.10 | - |
| 7 | 132 | Pfam | PF01464 | Transglycosylase SLT domain |
| 7 | 132 | InterPro | IPR008258 | Transglycosylase SLT domain 1 |
| 6 | 160 | PANTHER | PTHR37423 | SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED |
| 24 | 52 | ProSitePatterns | PS00922 | Prokaryotic transglycosylases signature. |
| 24 | 52 | InterPro | IPR000189 | Prokaryotic transglycosylase, active site |
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_W1DGZ0
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_01546
|
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 |
|---|---|---|---|---|---|---|---|
| 3 | 0.82 |
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 | 1.72 | 0.03 | ||||||
| 2 | 1.24 | 0.012 |