Protein profile

PA2678

ABC transporter permease

Genome: NC_002516.2

Gene: PA2678 Structure source: AlphaFold UniProt Q9I0G0
Amino acids 267
Annotations 6
Features 38
PDB binders 2
Druggability 0.458

Overview

Basic information about this protein and its source genome.

Accession
PA2678
Gene
PA2678
Status
annotated
Amino acids
267
Structure source
AlphaFold
GO
GO:0043190 A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter. GO:0140359 Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane. GO:0015920 The directed movement of lipopolysaccharides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. A lipopolysaccharide is any of a group of related, structurally complex components of the outer membrane of Gram-negative bacteria. Lipopolysaccharides consist three covalently linked regions, lipid A, core oligosaccharide, and an O side chain. Lipid A is responsible for the toxicity of the lipopolysaccharide. GO:0015774 The directed movement of polysaccharides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. A polysaccharide is a polymer of many (typically more than 10) monosaccharide residues linked glycosidically. GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

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 0.458
Structure
Pocket

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • GO:0043190 A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter.
  • GO:0140359 Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane.
  • GO:0015920 The directed movement of lipopolysaccharides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. A lipopolysaccharide is any of a group of related, structurally complex components of the outer membrane of Gram-negative bacteria. Lipopolysaccharides consist three covalently linked regions, lipid A, core oligosaccharide, and an O side chain. Lipid A is responsible for the toxicity of the lipopolysaccharide.
  • GO:0015774 The directed movement of polysaccharides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. A polysaccharide is a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
  • GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records
Show feature table
Start End DB Term Name
229 233 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
140 147 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
9 267 PANTHER PTHR30413 INNER MEMBRANE TRANSPORT PERMEASE
1 14 Phobius SIGNAL_PEPTIDE Signal peptide region
199 209 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
185 207 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
108 139 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
234 256 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
154 176 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
1 1 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
234 256 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
185 204 PRINTS PR00164 ABC-2 type transport system membrane protein signature
185 204 InterPro IPR000412 ABC-2 transporter
37 58 PRINTS PR00164 ABC-2 type transport system membrane protein signature
37 58 InterPro IPR000412 ABC-2 transporter
205 224 PRINTS PR00164 ABC-2 type transport system membrane protein signature
205 224 InterPro IPR000412 ABC-2 transporter
33 55 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
38 58 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
182 198 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
2 9 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
210 228 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
171 181 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
119 139 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
70 87 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
59 69 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
15 37 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
70 87 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
35 259 ProSiteProfiles PS51012 ABC transporter integral membrane type-2 domain profile.
35 259 InterPro IPR047817 ABC-2 type transporter, transmembrane domain, bacterial-type
88 118 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
10 14 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
4 260 PIRSF PIRSF006648 DrrB
4 260 InterPro IPR000412 ABC-2 transporter
257 267 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
148 170 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
17 228 Pfam PF01061 ABC-2 type transporter
17 228 InterPro IPR013525 ABC-2 type transporter, transmembrane 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

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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 PA2678
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
6 0.458
1 0.333
2 0.249

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.

33 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
LDA O67182 229.4 Da LogP 4.48 TPSA 23.1 ✓ Ro5 ✓ Clean CCCCCCCCCCCC[N+](C)(C)[O-]
P4G O67182 162.2 Da LogP 1.08 TPSA 27.7 ✓ Ro5 ✓ Clean CCOCCOCCOCC

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.