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ABC Transporters: Importer

ABC Transporters: Importer

ATP-binding cassette or ABC transporters are a class of ATP-driven pumps that hydrolyze ATP to move solutes across the membrane. They can be grouped into importers and exporters. While exporters are present in all domains of life, importers exist only in bacteria and some plants.
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:

ABC Transporters: Exporter

ABC Transporters: Exporter

ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...

Allosteric Proteins-ATCase

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

The ADP/ATP Carrier Protein

The ADP/ATP Carrier Protein

ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...

ATP Driven Pumps I: An Overview

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...

Membrane Asymmetry Regulating Transporters

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...

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Related Experiment Video

Updated: Jun 16, 2026

Microscopy-based Assays for High-throughput Screening of Host Factors Involved in Brucella Infection of Hela Cells

Microscopy-based Assays for High-throughput Screening of Host Factors Involved in Brucella Infection of Hela Cells

Published on: August 5, 2016

ATP-Binding Cassette Systems of Brucella.

Dominic C Jenner¹, Elie Dassa, Adrian M Whatmore

¹Department of Biomedical Sciences, Defence Science and Technology Laboratory, Porton Down, Salisbury, Wiltshire SP4 0JQ, UK.

Comparative and Functional Genomics

|February 20, 2010

Summary

This study compares ATP-binding cassette (ABC) systems in five Brucella species. Differences in these systems, especially those absent in Brucella ovis, may explain why it doesn't cause human brucellosis.

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Last Updated: Jun 16, 2026

Microscopy-based Assays for High-throughput Screening of Host Factors Involved in Brucella Infection of Hela Cells

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Published on: August 5, 2016

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Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Published on: November 29, 2014

Area of Science:

Microbiology
Genomics
Infectious Diseases

Background:

Brucellosis is a significant zoonotic disease with global prevalence.
ATP-binding cassette (ABC) systems are crucial for nutrient transport and virulence in bacteria.
Understanding these systems in Brucella species can reveal insights into pathogenesis.

Purpose of the Study:

To compile and compare inventories of functional ABC systems across five key Brucella species.
To identify specific differences in ABC systems that may correlate with virulence in human brucellosis.

Main Methods:

Bioinformatic analysis to identify and align putative functional ABC systems.
Comparative genomics of Brucella melitensis, Brucella abortus, Brucella canis, Brucella suis, and Brucella ovis genomes.

Main Results:

All studied Brucella species possess numerous ABC systems, particularly nutrient importers.
Significant variations in the total number of ABC systems were observed (e.g., B. melitensis: 79, B. ovis: 59).
Specific functional ABC systems differed among the species, with notable absences in B. ovis.

Conclusions:

Brucella species exhibit substantial diversity in their ABC systems.
Functional ABC systems absent in Brucella ovis may represent potential virulence factors for human brucellosis.
Further investigation into these specific ABC systems could identify novel therapeutic targets.