Protein profile

KP13_03579

putative pilin chaperone

Genome: KpKP13

Gene: AHE45922.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GT77
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Amino acids 228
Annotations 4
Features 32
PDB binders 3
Druggability 0.344

Overview

Basic information about this protein and its source genome.

Accession
KP13_03579
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45922.1
Status
annotated
Amino acids
228
Structure source
AlphaFold + ColabFold
GO
GO:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone. GO:0043711 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pilus, a short filamentous structure on a bacterial cell, flagella-like in structure and generally present in many copies. GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. 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.

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 (%)
41.631
DEG E-value
1.1e-45
Localization
Periplasmic
ColabFold pLDDT
89.2

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 0.344
Structure A0A0H3GT77
Pocket Pocket 3
P2Rank 0.037
Structure A0A0H3GT77
Pocket Pocket 1
ColabFold model
FPocket 0.458 · Pocket 3
P2Rank 0.112 · Pocket 1
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 4 / 4744 genomes with a hit
Normalized 0.001

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:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
  • GO:0043711 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pilus, a short filamentous structure on a bacterial cell, flagella-like in structure and generally present in many copies.
  • GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
  • 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.

32 records
Show feature table
Start End DB Term Name
133 224 SUPERFAMILY SSF49584 Periplasmic chaperone C-domain
133 224 InterPro IPR036316 Pili assembly chaperone, C-terminal domain superfamily
12 16 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
163 222 Pfam PF02753 Pili assembly chaperone PapD, C-terminal domain
163 222 InterPro IPR016148 Pili assembly chaperone, C-terminal
1 2 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
18 137 FunFam G3DSA:2.60.40.10:FF:000458 Molecular chaperone FimC
2 226 PANTHER PTHR30251 PILUS ASSEMBLY CHAPERONE
13 139 SUPERFAMILY SSF49354 PapD-like
13 139 InterPro IPR008962 PapD-like superfamily
1 16 SignalP_EUK SignalP-noTM SignalP-noTM
94 111 ProSitePatterns PS00635 Gram-negative pili assembly chaperone signature.
94 111 InterPro IPR018046 Pili assembly chaperone, conserved site
1 16 Phobius SIGNAL_PEPTIDE Signal peptide region
18 137 Gene3D G3DSA:2.60.40.10 Immunoglobulins
18 137 InterPro IPR013783 Immunoglobulin-like fold
17 228 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
18 139 Pfam PF00345 Pili and flagellar-assembly chaperone, PapD N-terminal domain
18 139 InterPro IPR016147 Pili assembly chaperone, N-terminal
3 11 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
95 112 PRINTS PR00969 Pili chaperone signature
95 112 InterPro IPR001829 Pili assembly chaperone, bacterial
67 88 PRINTS PR00969 Pili chaperone signature
67 88 InterPro IPR001829 Pili assembly chaperone, bacterial
121 136 PRINTS PR00969 Pili chaperone signature
121 136 InterPro IPR001829 Pili assembly chaperone, bacterial
158 173 PRINTS PR00969 Pili chaperone signature
158 173 InterPro IPR001829 Pili assembly chaperone, bacterial
18 27 PRINTS PR00969 Pili chaperone signature
18 27 InterPro IPR001829 Pili assembly chaperone, bacterial
142 224 Gene3D G3DSA:2.60.40.10 Immunoglobulins
142 224 InterPro IPR013783 Immunoglobulin-like fold

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_A0A0H3GT77
AlphaFold — — full sequence — Viewing
ColabFold KP13_03579
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 0.344

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 0.8 0.003

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.

3 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
EC2
2XG5
P15319 453.6 Da LogP 5.94 TPSA 59.3 1 viol. ✓ Clean c1ccc(cc1)[C@@H]2[C@H](N3C(=O)C=C(C(=C3S2)C4CC4…
EC5
2XG5
P15319 471.6 Da LogP 5.90 TPSA 79.5 1 viol. ✓ Clean c1ccc(cc1)C[C@@H](C(=O)O)N2C(=O)C=C(C(=C2SO)C3C…
XC2
2XG4
P15319 476.6 Da LogP 4.03 TPSA 71.8 ✓ Ro5 ✓ Clean c1ccc2c(c1)cccc2CC3=C(C(=O)N4[C@@H](CSC4=C3C5CC…

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.