Protein profile

KP13_04714

Nitrate/nitrite sensor protein narX

Genome: KpKP13

Gene: AHE44021.1 narX Structure source: AlphaFold + ColabFold UniProt A0A0H3GPN7
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Amino acids 592
Annotations 9
Features 39
PDB binders 2
Druggability 0.77

Overview

Basic information about this protein and its source genome.

Accession
KP13_04714
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE44021.1 narX
Status
annotated
Amino acids
592
Structure source
AlphaFold + ColabFold
EC
2.7.13.3
GO
GO:0004673 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0000160 A conserved series of molecular signals found in prokaryotes and eukaryotes; involves autophosphorylation of a histidine kinase and the transfer of the phosphate group to an aspartate that then acts as a phospho-donor to response regulator proteins. GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. GO:0000155 Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response. GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

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
CytoplasmicMembrane
ColabFold pLDDT
83.67

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 0.77
Structure A0A0H3GPN7
Pocket Pocket 10
P2Rank 0.443
Structure A0A0H3GPN7
Pocket Pocket 1
ColabFold model
FPocket 0.74 · Pocket 38
P2Rank 0.406 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 63 / 4744 genomes with a hit
Normalized 0.013

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:0004673 Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0000160 A conserved series of molecular signals found in prokaryotes and eukaryotes; involves autophosphorylation of a histidine kinase and the transfer of the phosphate group to an aspartate that then acts as a phospho-donor to response regulator proteins.
  • GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
  • GO:0000155 Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response.
  • GO:0007165 The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
  • GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Sequence Features

Domain/signature hits from InterPro and related databases.

39 records
Show feature table
Start End DB Term Name
499 583 CDD cd16917 HATPase_UhpB-NarQ-NarX-like
494 587 SMART SM00387 HKATPase_4
494 587 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
454 587 Gene3D G3DSA:3.30.565.10 -
454 587 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
4 583 PANTHER PTHR24421 NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED
176 228 SMART SM00304 HAMP_11
176 228 InterPro IPR003660 HAMP domain
393 587 ProSiteProfiles PS50109 Histidine kinase domain profile.
393 587 InterPro IPR005467 Histidine kinase domain
15 37 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
39 123 Pfam PF13675 Type IV pili methyl-accepting chemotaxis transducer N-term
39 123 InterPro IPR029095 NarX-like, N-terminal
176 228 ProSiteProfiles PS50885 HAMP domain profile.
173 224 Pfam PF00672 HAMP domain
173 224 InterPro IPR003660 HAMP domain
466 583 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
466 583 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
175 592 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
38 152 CDD cd22900 NarX_sensor
42 148 Gene3D G3DSA:1.20.120.960 Histidine kinase NarX, sensor domain
42 148 InterPro IPR042295 NarX-like, N-terminal domain superfamily
1 592 PIRSF PIRSF003167 HK_NarX/NarQ
1 592 InterPro IPR016380 Signal transduction histidine kinase, nitrate/nitrite-sensing
179 223 CDD cd06225 HAMP
1 33 Phobius SIGNAL_PEPTIDE Signal peptide region
177 225 SUPERFAMILY SSF158472 HAMP domain-like
26 33 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
357 450 Gene3D G3DSA:1.20.5.1930 -
390 453 Pfam PF07730 Histidine kinase
390 453 InterPro IPR011712 Signal transduction histidine kinase, subgroup 3, dimerisation and phosphoacceptor domain
152 174 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
175 254 Gene3D G3DSA:1.10.287.130 -
1 14 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
154 174 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
496 583 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
496 583 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
15 25 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
34 153 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular 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

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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_A0A0H3GPN7
AlphaFold — — full sequence — Viewing
ColabFold KP13_04714
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
10 0.77
18 0.711

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 4.06 0.163
2 2.92 0.093
3 2.44 0.066
4 1.1 0.008

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.

52 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
ACP
3EHJ
O34757 505.2 Da LogP -1.52 TPSA 269.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
LFA
5IJI
P27896 282.6 Da LogP 8.05 TPSA 0.0 1 viol. ✓ Clean CCCCCCCCCCCCCCCCCCCC

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.