KpATCC43816 Protein target profile

histidine kinase-, DNA gyrase B-, and HSP90-likeATPase family protein

Accession: VK055_2520

Gene: AIK81117.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GRK7

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Length 541

Pocket druggability (P2Rank · AlphaFold DB model) 0.777

Direct ligand evidence 0 20 total records

Functional annotation 0 EC 4 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.78, FPocket 0.93). Use the 3D pocket comparison to verify whether they identify the same site. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.93. This is a computational pocket signal, not binding validation. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: No hit
Gut microbiome similarity: 1.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 39.474 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 87.59 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.777

Structure A0A0H3GRK7

Pocket Pocket 1

Druggability (FPocket) 0.933

Structure A0A0H3GRK7

Pocket Pocket 7

ColabFold model

P2Rank 0.795 · Pocket 1

FPocket 0.916 · Pocket 5

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 48 / 4744 genomes with a hit

Prevalence 1.0%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKLSFQYKLFISLVAFFSVLFIALGIYYYFDASRQLYQEMSARAKIQAEEIALMPNLRQQVSRHDPQAIQAFMQQIAAHSDASFIVIGDRQGVHLFHSVHPEWVGTRLVGGDNQAVLEGKSITTIRKGGLGVSLRSKTPIVDDAGRVIGIVSVGYLTSYLDSITLTKVINIFIAAVLLLIALFIFSWYFTRSIKKQIFSLEPREIGLLVRQQKAMMESIFEGVIVIDRQRRIEVINHAARSLLGLSQPARQLRGQSIDSVISPQPFFASGDMLERDTHDELCRFNQLTVLASRVRIMLENTLQGWVITFRDRNEINALTAQLSQVKRYVDNLRIMRHEQLNRMTTLSGLLHMGHYDEAIRYIQAQSEHAQELLDFISSHFHSPTLCGLLLGKATRAREKGVALSFDPACRIDRPLPSLMESELISIIGNLLDNAIEATQRAELPHEPVEVLIQLNARELIIEVADRGVGIRPDIRERIFERGVTTKTRGDHGIGLYLIEHYVTQAGGTIEVADNAPRGTIFTLFIPADAHACPQPEVHDAS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: CytoplasmicMembrane

Gene Ontology (GO)

GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
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:0016310 The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
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.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

44 records

Show feature table

Start	End	DB	Term	Name
210	278	SMART	SM00091	pas_2
210	278	InterPro	IPR000014	PAS domain
34	159	Pfam	PF17203	Single cache domain 3
34	159	InterPro	IPR033463	Single cache domain 3
168	190	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
394	526	SUPERFAMILY	SSF55874	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
394	526	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
477	487	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
477	487	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
459	473	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
459	473	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
489	507	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
489	507	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
513	526	PRINTS	PR00344	Bacterial sensor protein C-terminal signature
513	526	InterPro	IPR004358	Signal transduction histidine kinase-related protein, C-terminal
197	312	Gene3D	G3DSA:3.30.450.20	PAS domain
423	526	CDD	cd16915	HATPase_DpiB-CitA-like
1	8	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
396	529	ProSiteProfiles	PS50109	Histidine kinase domain profile.
396	529	InterPro	IPR005467	Histidine kinase domain
313	374	Gene3D	G3DSA:1.10.287.130	-
321	372	Pfam	PF14689	Sensor_kinase_SpoOB-type, alpha-helical domain
321	372	InterPro	IPR039506	SpoOB, alpha-helical domain
221	275	CDD	cd00130	PAS
221	275	InterPro	IPR000014	PAS domain
32	160	Gene3D	G3DSA:3.30.450.20	PAS domain
210	311	SUPERFAMILY	SSF55785	PYP-like sensor domain (PAS domain)
210	311	InterPro	IPR035965	PAS domain superfamily
9	30	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
388	532	Gene3D	G3DSA:3.30.565.10	-
388	532	InterPro	IPR036890	Histidine kinase/HSP90-like ATPase superfamily
34	164	SUPERFAMILY	SSF103190	Sensory domain-like
34	164	InterPro	IPR029151	Periplasmic sensor-like domain superfamily
322	372	SUPERFAMILY	SSF55890	Sporulation response regulatory protein Spo0B
322	372	InterPro	IPR016120	Signal transduction histidine kinase, sporulation regulator SpoOB
10	30	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
418	529	SMART	SM00387	HKATPase_4
418	529	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
421	527	Pfam	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
421	527	InterPro	IPR003594	Histidine kinase/HSP90-like ATPase
31	167	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
168	189	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
190	541	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
420	529	PANTHER	PTHR45436	SENSOR HISTIDINE KINASE YKOH

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.777

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Surrounding area

Pocket 2 P2Rank #2

0.652

Likely same site as FPocket 1 0.6 Å 16 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.056

Likely same site as FPocket 7 2.8 Å 8 shared residues 89% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.019

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #7

0.933

Likely same site as P2Rank 3 2.8 Å 8 shared residues 89% of smaller site

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Surrounding area

Pocket 2 FPocket #2

0.585

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Surrounding area

Pocket 3 FPocket #1

0.21

Likely same site as P2Rank 2 0.6 Å 16 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.795

Likely same site as FPocket 2 4.7 Å 20 shared residues 95% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.705

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Surrounding area

Pocket 3 P2Rank #3

0.265

Likely same site as FPocket 3 4.1 Å 13 shared residues 76% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.136

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Surrounding area

Pocket 5 P2Rank #5

0.086

Likely same site as FPocket 5 3.3 Å 8 shared residues 89% of smaller site

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #5

0.916

Likely same site as P2Rank 5 3.3 Å 8 shared residues 89% of smaller site

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Surrounding area

Pocket 2 FPocket #3

0.728

Likely same site as P2Rank 3 4.1 Å 13 shared residues 76% of smaller site

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Surrounding area

Pocket 3 FPocket #2

0.291

Likely same site as P2Rank 1 4.7 Å 20 shared residues 95% of smaller site

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GRK7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2520	ColabFold	—	—	full sequence	—	Loaded

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.

20 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 17 similarity-based ZINC candidates

Best available ligand signal

FLC PDB via homolog 189.1 Da · LogP -5.25 · TPSA 140.6 Open detail RCSB PDB

MO7 PDB via homolog Detail RCSB PDB

OMO PDB via homolog Detail RCSB PDB

ZINC1532902 ZINC proposed compound · Tanimoto 0.700 Detail ZINC

ZINC2018106 ZINC proposed compound · Tanimoto 0.700 Detail ZINC

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
FLC RCSB PDB	1P0Z	P52687	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
MO7 RCSB PDB	1P0Z	P52687	—	—	—	`[O-][Mo]123(=O)O[Mo]45(=O)(O16[Mo]7(=O)(O2)(O[M…`
OMO RCSB PDB	1P0Z	P52687	146.0 Da LogP -1.24 TPSA 57.5	✓ Ro5	✓ Clean	`O[Mo+6](=O)O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315135 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC1850353 ZINC	0.556	206.1 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC(O)(CC(=O)O)CC(=O)O`
ZINC13398014 ZINC	0.522	220.2 Da LogP -1.07 TPSA 110.1	✓ Ro5	✓ Clean	`COC(=O)CC(O)(CC(=O)OC)C(=O)O`
ZINC3861629 ZINC	0.522	206.1 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C(O)(CC(=O)O)CC(=O)O`
ZINC100969993 ZINC	0.500	359.5 Da LogP 2.70 TPSA 123.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC100969996 ZINC	0.500	359.5 Da LogP 2.70 TPSA 123.9	✓ Ro5	✓ Clean	`CCCCCCCCCCCCNC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC1711854 ZINC	0.500	248.2 Da LogP -0.13 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)CC(CC(=O)O)(CC(=O)O)CC(=O)O`

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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GRK7