Protein profile

KP13_02201

putative lipoprotein

Genome: KpKP13

Gene: AHE42770.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GY33
Amino acids 246
Annotations 4
Features 29
PDB binders 3
Druggability 0.214

Overview

Basic information about this protein and its source genome.

Accession
KP13_02201
Gene
AHE42770.1
Status
annotated
Amino acids
246
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 (%)
40.833
DEG E-value
2.14e-21
Localization
OuterMembrane
ColabFold pLDDT
79.85

Selected Druggability evidence

AlphaFold / UniProt model

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.

FPocket 0.214
Structure A0A0H3GY33
Pocket Pocket 13
P2Rank 0.724
Structure A0A0H3GY33
Pocket Pocket 1
ColabFold model
FPocket 0.368 · Pocket 1
P2Rank 0.567 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 77 / 4744 genomes with a hit
Normalized 0.016

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

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.

29 records
Show feature table
Start End DB Term Name
38 81 CDD cd00118 LysM
38 81 InterPro IPR018392 LysM domain
97 238 PANTHER PTHR21666 PEPTIDASE-RELATED
82 109 MobiDBLite mobidb-lite consensus disorder prediction
28 32 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
12 246 NCBIfam NF040883 amidase activator ActS
37 77 FunFam G3DSA:3.10.350.10:FF:000006 YgeR family lipoprotein
17 27 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
1 27 SignalP_EUK SignalP-noTM SignalP-noTM
78 238 FunFam G3DSA:2.70.70.10:FF:000005 Hypothetical lipoprotein YgeR
140 224 CDD cd12797 M23_peptidase
33 246 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
37 77 Gene3D G3DSA:3.10.350.10 LysM domain
37 77 InterPro IPR036779 LysM domain superfamily
39 237 SUPERFAMILY SSF51261 Duplicated hybrid motif
39 237 InterPro IPR011055 Duplicated hybrid motif
1 16 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
1 21 SignalP_GRAM_POSITIVE SignalP-TM SignalP-TM
78 238 Gene3D G3DSA:2.70.70.10 Glucose Permease (Domain IIA)
78 238 InterPro IPR011055 Duplicated hybrid motif
39 81 Pfam PF01476 LysM domain
39 81 InterPro IPR018392 LysM domain
38 82 SMART SM00257 LysM_2
38 82 InterPro IPR018392 LysM domain
37 81 ProSiteProfiles PS51782 LysM domain profile.
37 81 InterPro IPR018392 LysM domain
140 233 Pfam PF01551 Peptidase family M23
140 233 InterPro IPR016047 Peptidase M23
1 32 Phobius SIGNAL_PEPTIDE Signal peptide region

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GY33
AlphaFold full sequence Viewing
ColabFold KP13_02201
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
13 0.214

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 7.52 0.396
2 2.01 0.043

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

22 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
4SQ O33599 281.2 Da LogP -2.12 TPSA 158.8 ✓ Ro5 ✓ Clean C(CP(=O)(CNC(=O)CN)O)C(=O)NCC(=O)O
CAC O33599 137.0 Da LogP -0.52 TPSA 40.1 ✓ Ro5 ✓ Clean C[As](=O)(C)[O-]
TLA O33599 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=O)O)O

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.