Protein profile

KP13_31576

Multidrug resistance protein A

Genome: KpKP13

Gene: AHE43071.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GWJ4
Amino acids 390
Annotations 6
Features 18
PDB binders 0
Druggability 0.085

Overview

Basic information about this protein and its source genome.

Accession
KP13_31576
Gene
AHE43071.1
Status
annotated
Amino acids
390
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
50.535
DEG E-value
7.37e-125
Localization
CytoplasmicMembrane
ColabFold pLDDT
91.78

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 0.085
Structure A0A0H3GWJ4
Pocket Pocket 2
P2Rank 0.004
Structure A0A0H3GWJ4
Pocket Pocket 1
ColabFold model
FPocket 0.132 · Pocket 16
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 124 / 4744 genomes with a hit
Normalized 0.026

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:1990961 A process that reduces or removes the toxicity of a xenobiotic by exporting it outside the cell.
  • GO:0042910 Enables the directed movement of a xenobiotic from one side of a membrane to the other. A xenobiotic is a compound foreign to the organism exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
  • GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
  • 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:0015721 The directed movement of bile acid and bile salts into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0046677 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records
Show feature table
Start End DB Term Name
56 113 SUPERFAMILY SSF111369 HlyD-like secretion proteins
61 124 Gene3D G3DSA:2.40.50.100 -
23 44 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
36 345 Pfam PF00529 Cation efflux system protein CusB domain 1
36 345 InterPro IPR043602 Cation efflux system protein CusB, domain 1
160 180 Coils Coil Coil
1 361 PANTHER PTHR30386 MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP
194 270 SUPERFAMILY SSF111369 HlyD-like secretion proteins
234 354 Gene3D G3DSA:2.40.30.170 -
23 45 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
232 354 FunFam G3DSA:2.40.30.170:FF:000003 Multidrug resistance protein A
170 289 Pfam PF16576 Barrel-sandwich domain of CusB or HlyD membrane-fusion
170 289 InterPro IPR032317 RND efflux pump, membrane fusion protein, barrel-sandwich domain
20 345 NCBIfam TIGR00998 EmrA/EmrK family multidrug efflux transporter periplasmic adaptor subunit
20 345 InterPro IPR005694 Membrane fusion proteins, proteobacteria
45 390 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
122 142 Coils Coil Coil
1 22 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.

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

No pockets are loaded yet for the displayed AlphaFold model AF_A0A0H3GWJ4 structure. Run experimental pocket backfill to show FPocket/P2Rank overlays on this structure.

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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_A0A0H3GWJ4
AlphaFold full sequence Viewing
ColabFold KP13_31576
ColabFold full sequence Loaded