Protein profile

KP13_00380

LexA repressor

Genome: KpKP13

Gene: lexA AHE46881.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQ57
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Amino acids 202
Annotations 9
Features 26
PDB binders 0
Druggability 0.237

Overview

Basic information about this protein and its source genome.

Accession
KP13_00380
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
lexA AHE46881.1
Status
annotated
Amino acids
202
Structure source
AlphaFold + ColabFold
EC
3.4.21.88
GO
GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. GO:0009432 An error-prone process for repairing damaged microbial DNA. GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). GO:0045892 Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).

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 (%)
94.554
DEG E-value
6.32e-141
Localization
Cytoplasmic
ColabFold pLDDT
90.8

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 0.237
Structure A0A0H3GQ57
Pocket Pocket 5
P2Rank 0.104
Structure A0A0H3GQ57
Pocket Pocket 1
ColabFold model
FPocket 0.466 · Pocket 6
P2Rank 0.072 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 167 / 4744 genomes with a hit
Normalized 0.035

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0006355 Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
  • GO:0009432 An error-prone process for repairing damaged microbial DNA.
  • GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
  • GO:0045892 Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
  • GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
  • GO:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
  • GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
  • GO:0006260 The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records
Show feature table
Start End DB Term Name
1 199 NCBIfam TIGR00498 transcriptional repressor LexA
1 199 InterPro IPR006200 Transcription regulator LexA
77 192 Pfam PF00717 Peptidase S24-like
77 192 InterPro IPR015927 Peptidase S24/S26A/S26B/S26C
1 198 PANTHER PTHR33516 LEXA REPRESSOR
111 180 CDD cd06529 S24_LexA-like
111 180 InterPro IPR039418 LexA-like
3 69 SUPERFAMILY SSF46785 Winged helix DNA-binding domain
3 69 InterPro IPR036390 Winged helix DNA-binding domain superfamily
75 199 FunFam G3DSA:2.10.109.10:FF:000001 LexA repressor
3 199 Hamap MF_00015 LexA repressor [lexA].
3 199 InterPro IPR006200 Transcription regulator LexA
75 202 Gene3D G3DSA:2.10.109.10 Umud Fragment, subunit A
75 198 SUPERFAMILY SSF51306 LexA/Signal peptidase
75 198 InterPro IPR036286 LexA/Signal peptidase-like superfamily
111 121 PRINTS PR00726 Repressor LexA serine protease (S24) family signature
111 121 InterPro IPR006197 Peptidase S24, LexA-like
150 162 PRINTS PR00726 Repressor LexA serine protease (S24) family signature
150 162 InterPro IPR006197 Peptidase S24, LexA-like
122 133 PRINTS PR00726 Repressor LexA serine protease (S24) family signature
122 133 InterPro IPR006197 Peptidase S24, LexA-like
1 69 Gene3D G3DSA:1.10.10.10 -
1 69 InterPro IPR036388 Winged helix-like DNA-binding domain superfamily
1 69 FunFam G3DSA:1.10.10.10:FF:000009 LexA repressor
1 65 Pfam PF01726 LexA DNA binding domain
1 65 InterPro IPR006199 LexA repressor, DNA-binding domain

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_A0A0H3GQ57
AlphaFold — — full sequence — Viewing
ColabFold KP13_00380
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
5 0.237

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 1.98 0.042