Protein profile

PA3007

LexA repressor

Genome: NC_002516.2

Gene: lexA PA3007 Structure source: Experimental + AlphaFold UniProt P37452
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Amino acids 204
Annotations 12
Features 26
PDB binders 0
Druggability 0.317

Overview

Basic information about this protein and its source genome.

Accession
PA3007
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
lexA PA3007
Status
annotated
Amino acids
204
Structure source
Experimental + AlphaFold
EC
3.4.21.88
GO
GO:0032993 A macromolecular complex containing both protein and DNA molecules. GO:0001217 A DNA-binding transcription factor activity that represses or decreases the transcription of specific gene sets. GO:0043565 Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. 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: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.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

Selected Druggability evidence

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 0.317
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

11
  • GO:0032993 A macromolecular complex containing both protein and DNA molecules.
  • GO:0001217 A DNA-binding transcription factor activity that represses or decreases the transcription of specific gene sets.
  • GO:0043565 Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.
  • 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: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.
  • 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: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:0003677 Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).

Sequence Features

Domain/signature hits from InterPro and related databases.

26 records
Show feature table
Start End DB Term Name
117 193 CDD cd06529 S24_LexA-like
117 193 InterPro IPR039418 LexA-like
1 204 NCBIfam TIGR00498 transcriptional repressor LexA
1 204 InterPro IPR006200 Transcription regulator LexA
81 204 FunFam G3DSA:2.10.109.10:FF:000001 LexA repressor
3 70 SUPERFAMILY SSF46785 Winged helix DNA-binding domain
3 70 InterPro IPR036390 Winged helix 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
1 68 Gene3D G3DSA:1.10.10.10 -
1 68 InterPro IPR036388 Winged helix-like DNA-binding domain superfamily
117 127 PRINTS PR00726 Repressor LexA serine protease (S24) family signature
117 127 InterPro IPR006197 Peptidase S24, LexA-like
128 139 PRINTS PR00726 Repressor LexA serine protease (S24) family signature
128 139 InterPro IPR006197 Peptidase S24, LexA-like
156 168 PRINTS PR00726 Repressor LexA serine protease (S24) family signature
156 168 InterPro IPR006197 Peptidase S24, LexA-like
83 196 Pfam PF00717 Peptidase S24-like
83 196 InterPro IPR015927 Peptidase S24/S26A/S26B/S26C
82 203 SUPERFAMILY SSF51306 LexA/Signal peptidase
82 203 InterPro IPR036286 LexA/Signal peptidase-like superfamily
81 204 Gene3D G3DSA:2.10.109.10 Umud Fragment, subunit A
3 204 Hamap MF_00015 LexA repressor [lexA].
3 204 InterPro IPR006200 Transcription regulator LexA
1 203 PANTHER PTHR33516 LEXA REPRESSOR

3D Structure

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

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Structural evidence

1 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 8B0V
X-ray 1.70 Å A,B
60.8% 81-204
PDBe RCSB PDBj File
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AlphaFold PA3007
AlphaFold — — full sequence — Loaded
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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 0.317