Protein profile

KP13_05220

Chaperone protein lpfB

Genome: KpKP13

Gene: AHE44627.1 lpfB Structure source: AlphaFold + ColabFold UniProt A0A0H3GNA0
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Amino acids 231
Annotations 4
Features 33
PDB binders 3
Druggability 0.379

Overview

Basic information about this protein and its source genome.

Accession
KP13_05220
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE44627.1 lpfB
Status
annotated
Amino acids
231
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)
N
DEG identity (%)
0.0
Localization
Periplasmic
ColabFold pLDDT
88.81

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 0.379
Structure A0A0H3GNA0
Pocket Pocket 6
P2Rank 0.027
Structure A0A0H3GNA0
Pocket Pocket 1
ColabFold model
FPocket 0.756 · Pocket 10
P2Rank 0.036 · Pocket 1
Core conservation Accessory gene
Roary core
CoreCruncher accessory
Gut microbiome 3 / 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.

33 records
Show feature table
Start End DB Term Name
23 140 Pfam PF00345 Pili and flagellar-assembly chaperone, PapD N-terminal domain
23 140 InterPro IPR016147 Pili assembly chaperone, N-terminal
1 5 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
96 113 ProSitePatterns PS00635 Gram-negative pili assembly chaperone signature.
96 113 InterPro IPR018046 Pili assembly chaperone, conserved site
1 21 SignalP_GRAM_POSITIVE SignalP-TM SignalP-TM
24 138 Gene3D G3DSA:2.60.40.10 Immunoglobulins
24 138 InterPro IPR013783 Immunoglobulin-like fold
142 224 SUPERFAMILY SSF49584 Periplasmic chaperone C-domain
142 224 InterPro IPR036316 Pili assembly chaperone, C-terminal domain superfamily
6 17 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
22 231 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 21 Phobius SIGNAL_PEPTIDE Signal peptide region
1 21 SignalP_EUK SignalP-noTM SignalP-noTM
157 172 PRINTS PR00969 Pili chaperone signature
157 172 InterPro IPR001829 Pili assembly chaperone, bacterial
97 114 PRINTS PR00969 Pili chaperone signature
97 114 InterPro IPR001829 Pili assembly chaperone, bacterial
122 137 PRINTS PR00969 Pili chaperone signature
122 137 InterPro IPR001829 Pili assembly chaperone, bacterial
24 33 PRINTS PR00969 Pili chaperone signature
24 33 InterPro IPR001829 Pili assembly chaperone, bacterial
69 90 PRINTS PR00969 Pili chaperone signature
69 90 InterPro IPR001829 Pili assembly chaperone, bacterial
7 29 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
5 224 PANTHER PTHR30251 PILUS ASSEMBLY CHAPERONE
142 226 Gene3D G3DSA:2.60.40.10 Immunoglobulins
142 226 InterPro IPR013783 Immunoglobulin-like fold
18 21 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
18 140 SUPERFAMILY SSF49354 PapD-like
18 140 InterPro IPR008962 PapD-like superfamily

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_A0A0H3GNA0
AlphaFold — — full sequence — Viewing
ColabFold KP13_05220
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
6 0.379

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 0.72 0.002

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.