Protein profile

PA4102

protein BfmS

Genome: NC_002516.2

Gene: bfmS PA4102 Structure source: AlphaFold UniProt Q9HWS6
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Amino acids 434
Annotations 8
Features 39
PDB binders 2
Druggability 0.669

Overview

Basic information about this protein and its source genome.

Accession
PA4102
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
bfmS PA4102
Status
annotated
Amino acids
434
Structure source
AlphaFold
EC
2.7.13.3
GO
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. 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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. 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:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
CytoplasmicMembrane

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 0.669
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MKLAVPRPRSLAARLALILFAGLVLAYGLSFASQFYERYQTAKHMMLDSLEQDVAISVAMLDRLTPAEREAWLPRLERRTYRYRLDAGEPGQPLALADAPVAAHSIERALDGQYPLTLRTVADSRPHFQVLLRLRDGSPLTIDVTPAPVPLSGWLPLVLLVQLLLLLLCTGLAVRTAIGPLTRLVKAVEHLDPNRPAQPLAETGPREVAHAAAAFNAMQARIADYLKERMQLLAAISHDLQTPITRMKLRVEFMDASSDRDKLWNDLEEMQHLVREGVAYARSMHGSTETSCRVDLDAFLDSLVFDYQDSGKQVQLDGRTGAVIDTRPHALRRVLVNLVDNALKFAGAARLEVERRTDGGTRIQVLDNGPGIPAEELDEVLKPFYRVENSRNRDTGGTGLGLAIAQQLSLALGGRLTLANRAGGGLCARIELDP

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • 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.
  • 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:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • 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:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

39 records
Show feature table
Start End DB Term Name
396 414 PRINTS PR00344 Bacterial sensor protein C-terminal signature
396 414 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
361 375 PRINTS PR00344 Bacterial sensor protein C-terminal signature
361 375 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
379 389 PRINTS PR00344 Bacterial sensor protein C-terminal signature
379 389 InterPro IPR004358 Signal transduction histidine kinase-related protein, C-terminal
1 32 Phobius SIGNAL_PEPTIDE Signal peptide region
152 174 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
15 27 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
287 433 FunFam G3DSA:3.30.565.10:FF:000253 Two-component sensor histidine kinase
329 433 Pfam PF02518 Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
329 433 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
28 32 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
154 174 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
33 153 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
10 32 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
326 434 SMART SM00387 HKATPase_4
326 434 InterPro IPR003594 Histidine kinase/HSP90-like ATPase
292 432 SUPERFAMILY SSF55874 ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
292 432 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
212 282 SUPERFAMILY SSF47384 Homodimeric domain of signal transducing histidine kinase
212 282 InterPro IPR036097 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily
7 434 PANTHER PTHR44936 SENSOR PROTEIN CREC
228 286 SMART SM00388 HisKA_10
228 286 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
175 227 ProSiteProfiles PS50885 HAMP domain profile.
175 227 InterPro IPR003660 HAMP domain
226 276 CDD cd00082 HisKA
226 276 InterPro IPR003661 Signal transduction histidine kinase, dimerisation/phosphoacceptor domain
175 227 SMART SM00304 HAMP_11
172 280 Gene3D G3DSA:1.10.287.130 -
1 14 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
175 434 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
235 434 ProSiteProfiles PS50109 Histidine kinase domain profile.
235 434 InterPro IPR005467 Histidine kinase domain
287 433 Gene3D G3DSA:3.30.565.10 -
287 433 InterPro IPR036890 Histidine kinase/HSP90-like ATPase superfamily
173 222 Pfam PF00672 HAMP domain
173 222 InterPro IPR003660 HAMP domain

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

0 + 1

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA4102
AlphaFold — — full sequence — Viewing
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
1 0.669
4 0.388
16 0.267

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
ANP
4BIW
P0AE82 506.2 Da LogP -2.06 TPSA 281.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
RDC
3CGY
P0DM80 364.8 Da LogP 2.69 TPSA 96.4 ✓ Ro5 ✓ Clean C[C@@H]1C[C@@H]2[C@H](O2)\C=C/C=C/C(=O)Cc3c(c(c…

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.