Protein profile

PA3888

ABC transporter permease

Genome: NC_002516.2

Gene: PA3888 Structure source: AlphaFold UniProt Q9HXC5
Amino acids 240
Annotations 9
Features 32
PDB binders 3
Druggability 0.975

Overview

Basic information about this protein and its source genome.

Accession
PA3888
Gene
PA3888
Status
annotated
Amino acids
240
Structure source
AlphaFold
GO
GO:0055052 A complex for the transport of metabolites into the cell, consisting of 5 subunits: two ATP-binding subunits, two membrane spanning subunits, and one substrate-binding subunit. In organisms with two membranes, the substrate-binding protein moves freely in the periplasmic space and joins the other subunits only when bound with substrate. In organisms with only one membrane the substrate-binding protein is tethered to the cytoplasmic membrane and associated with the other subunits. Transport of the substrate across the membrane is driven by the hydrolysis of ATP. 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:1902495 A transmembrane protein complex which enables the transfer of a substance from one side of a membrane to the other. GO:0015226 Enables the transfer of carnitine across a membrane. Carnitine is a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane. GO:0015838 The directed movement of betaine, the N-trimethyl derivative of an amino acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. GO:0071475 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.

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 0.975
Structure
Pocket

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Gene Ontology (GO)

9
  • GO:0055052 A complex for the transport of metabolites into the cell, consisting of 5 subunits: two ATP-binding subunits, two membrane spanning subunits, and one substrate-binding subunit. In organisms with two membranes, the substrate-binding protein moves freely in the periplasmic space and joins the other subunits only when bound with substrate. In organisms with only one membrane the substrate-binding protein is tethered to the cytoplasmic membrane and associated with the other subunits. Transport of the substrate across the membrane is driven by the hydrolysis of ATP.
  • 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:1902495 A transmembrane protein complex which enables the transfer of a substance from one side of a membrane to the other.
  • GO:0015226 Enables the transfer of carnitine across a membrane. Carnitine is a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane.
  • GO:0015838 The directed movement of betaine, the N-trimethyl derivative of an amino acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0071475 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, an increase in the concentration of salt (particularly but not exclusively sodium and chloride ions) in the environment.
  • GO:0031460 The directed movement of glycine betaine, N-trimethylglycine, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records
Show feature table
Start End DB Term Name
8 23 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
1 7 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
180 199 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
227 240 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
24 28 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
29 43 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
89 111 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
35 230 FunFam G3DSA:1.10.3720.10:FF:000001 Glycine betaine ABC transporter, permease
200 204 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
9 31 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
178 200 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
123 155 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
42 192 CDD cd06261 TM_PBP2
42 192 InterPro IPR000515 ABC transporter type 1, transmembrane domain MetI-like
44 68 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
60 230 Pfam PF00528 Binding-protein-dependent transport system inner membrane component
60 230 InterPro IPR000515 ABC transporter type 1, transmembrane domain MetI-like
37 221 SUPERFAMILY SSF161098 MetI-like
37 221 InterPro IPR035906 MetI-like superfamily
69 88 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
36 233 Gene3D G3DSA:1.10.3720.10 -
36 233 InterPro IPR035906 MetI-like superfamily
89 122 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
205 227 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
46 68 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
42 227 ProSiteProfiles PS50928 ABC transporter integral membrane type-1 domain profile.
42 227 InterPro IPR000515 ABC transporter type 1, transmembrane domain MetI-like
205 226 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
1 28 Phobius SIGNAL_PEPTIDE Signal peptide region
174 179 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
35 234 PANTHER PTHR30177 GLYCINE BETAINE/L-PROLINE TRANSPORT SYSTEM PERMEASE PROTEIN PROW
156 173 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.

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

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA3888
AlphaFold full sequence Viewing
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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
2 0.975
4 0.781
1 0.366
3 0.329

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.

53 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
2BA A0A0V8ETW8 658.4 Da LogP -1.63 TPSA 309.7 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@H]4[C@H](O3)C…
ANP A0A0V8ETW8 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)…
BET A0A0V8ETW8 118.2 Da LogP -0.22 TPSA 37.3 ✓ Ro5 ✓ Clean C[N+](C)(C)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.