Protein profile

KP13_03820

TPR repeat-containing protein

Genome: KpKP13

Gene: AHE43304.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GW14
Amino acids 487
Annotations 10
Features 19
PDB binders 0
Druggability 0.818

Overview

Basic information about this protein and its source genome.

Accession
KP13_03820
Gene
AHE43304.1
Status
annotated
Amino acids
487
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
88.26

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 0.818
Structure A0A0H3GW14
Pocket Pocket 31
P2Rank 0.424
Structure A0A0H3GW14
Pocket Pocket 1
ColabFold model
FPocket 0.725 · Pocket 30
P2Rank 0.281 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 110 / 4744 genomes with a hit
Normalized 0.023

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • 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.
  • GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0005515 Binding to a protein.
  • GO:0008237 Catalysis of the hydrolysis of peptide bonds 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.
  • 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: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:0008270 Binding to a zinc ion (Zn).
  • GO:0051603 OBSOLETE. The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records
Show feature table
Start End DB Term Name
313 428 SUPERFAMILY SSF48452 TPR-like
313 428 InterPro IPR011990 Tetratricopeptide-like helical domain superfamily
4 484 Hamap MF_00997 Beta-barrel assembly-enhancing protease [bepA].
4 484 InterPro IPR030873 Beta-barrel assembly-enhancing protease
1 7 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
75 150 Gene3D G3DSA:3.30.2010.10 Metalloproteases ("zincins"), catalytic domain
354 418 Pfam PF14559 Tetratricopeptide repeat
79 259 Pfam PF01435 Peptidase family M48
79 259 InterPro IPR001915 Peptidase M48
48 262 CDD cd07333 M48C_bepA_like
28 487 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 27 SignalP_EUK SignalP-noTM SignalP-noTM
269 483 Gene3D G3DSA:1.25.40.10 Tetratricopeptide repeat domain
269 483 InterPro IPR011990 Tetratricopeptide-like helical domain superfamily
1 27 SignalP_GRAM_POSITIVE SignalP-TM SignalP-TM
20 27 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
5 265 PANTHER PTHR22726 METALLOENDOPEPTIDASE OMA1
8 19 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
1 27 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

Loading 3D structure...

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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_A0A0H3GW14
AlphaFold full sequence Viewing
ColabFold KP13_03820
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
31 0.818
3 0.652
1 0.203

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 5.23 0.243
2 4.37 0.183
3 3.89 0.153
4 3.33 0.118
5 2.83 0.088