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The Escherichia coli ATP-binding cassette (ABC) proteins
1CRC Drug Resistance Group, Nuffield Department of Clinical Biochemistry and Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, University of Oxford, UK. linton@icrf.icnet
Molecular Microbiology
|May 21, 1998
Summary
The Escherichia coli genome encodes 79 ATP-binding cassette (ABC) proteins, the largest protein family. These proteins, primarily transporters, reveal insights into their evolution and function.
Area of Science:
- Microbiology
- Molecular Biology
- Genomics
Background:
- The completion of the Escherichia coli genome sequence enabled comprehensive analysis of its encoded proteins.
- ATP-binding cassette (ABC) proteins represent a significant functional group within bacterial proteomes.
Purpose of the Study:
- To identify and characterize all genomically encoded ATP-binding cassette (ABC) proteins in Escherichia coli.
- To analyze the distribution, function, and evolutionary relationships of ABC proteins and their domains.
Main Methods:
- Bioinformatic analysis of the Escherichia coli genome sequence.
- Identification and classification of ABC domains and associated proteins.
- Phylogenetic analysis of ABC protein families.
Main Results:
- Identified 79 distinct ABC proteins, comprising 97 ABC domains, forming the largest paralogous family in E. coli.
- Determined that 57 ABC systems function as transporters (44 uptake, 13 exporters), utilizing nearly 5% of the genome.
- Phylogenetic analysis revealed 10 major subfamilies of ABC proteins, offering insights into their evolutionary trajectories.
Conclusions:
- The extensive ABC protein repertoire in E. coli underscores their critical roles in cellular functions, particularly transport.
- The study provides a foundational understanding of ABC protein evolution and functional diversification within a model bacterium.