Protein profile
KP13_04897
Peptidoglycan-binding lysin domain-containing protein
Genome: KpKP13
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_04897
- Gene
- AHE45257.1
- Status
- annotated
- Amino acids
- 281
- 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 (%)
- 41.379
- DEG E-value
- 2.11e-63
- Localization
- Unknown
- ColabFold pLDDT
- 94.41
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)
8- GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
- GO:0005576 The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
- 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:0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
- GO:0071972 Catalysis of the reaction: 2 a peptidoglycan dimer (tetrapeptide) + 3 H2O = a peptidoglycan tetramer with L,D cross-links (L-Lys-D-Asn-L-Lys) + di-trans,poly-cis-undecaprenyl diphosphate + 4 D-alanine.
- 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.
- GO:0018104 The process of covalently linking peptidoglycan (murein) to proteins.
- GO:0008360 Any process that modulates the surface configuration of a cell.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 5 | 50 | CDD | cd00118 | LysM |
| 5 | 50 | InterPro | IPR018392 | LysM domain |
| 58 | 201 | FunFam | G3DSA:2.40.440.10:FF:000001 | L,D-transpeptidase YbiS |
| 6 | 51 | Gene3D | G3DSA:3.10.350.10 | LysM domain |
| 6 | 51 | InterPro | IPR036779 | LysM domain superfamily |
| 64 | 200 | Pfam | PF03734 | L,D-transpeptidase catalytic domain |
| 64 | 200 | InterPro | IPR005490 | L,D-transpeptidase catalytic domain |
| 6 | 51 | SUPERFAMILY | SSF54106 | LysM domain |
| 64 | 201 | CDD | cd16913 | YkuD_like |
| 64 | 201 | InterPro | IPR005490 | L,D-transpeptidase catalytic domain |
| 5 | 51 | SMART | SM00257 | LysM_2 |
| 5 | 51 | InterPro | IPR018392 | LysM domain |
| 7 | 51 | Pfam | PF01476 | LysM domain |
| 7 | 51 | InterPro | IPR018392 | LysM domain |
| 5 | 50 | ProSiteProfiles | PS51782 | LysM domain profile. |
| 1 | 55 | FunFam | G3DSA:3.10.350.10:FF:000007 | Probable L,D-transpeptidase YcfS |
| 62 | 200 | SUPERFAMILY | SSF141523 | L,D-transpeptidase catalytic domain-like |
| 62 | 200 | InterPro | IPR038063 | L,D-transpeptidase catalytic domain-like |
| 59 | 201 | Gene3D | G3DSA:2.40.440.10 | - |
| 59 | 201 | InterPro | IPR038063 | L,D-transpeptidase catalytic domain-like |
| 204 | 270 | Pfam | PF17969 | L,D-transpeptidase C-terminal domain |
| 204 | 270 | InterPro | IPR041597 | L,D-transpeptidase C-terminal domain |
| 4 | 209 | PANTHER | PTHR30582 | L,D-TRANSPEPTIDASE |
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_A0A447S5P8
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_04897
|
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 | 0.668 |
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 | 16.81 | 0.788 |
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 |
|---|---|---|---|---|---|---|---|
| 4 | 0.42 | ||||||
| 13 | 0.205 |
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 | 16.79 | 0.787 | ||||||
| 2 | 1.4 | 0.018 |