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PMID: 8302219 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

ABC transporters: bacterial exporters.

Microbiological reviews ·Vol. 57 ·No. 4 ·1993-12-00 ·Pages 995-1017

Fath MJ, Kolter R

Abstract

The ABC transporters (also called traffic ATPases) make up a large superfamily of proteins which share a common function and a common ATP-binding domain. ABC transporters are classified into three major groups: bacterial importers (the periplasmic permeases), eukaryotic transporters, and bacterial exporters. We present a comprehensive review of the bacterial ABC exporter group, which currently includes over 40 systems. The bacterial ABC exporter systems are functionally subdivided on the basis of the type of substrate that each translocates. We describe three main groups: protein exporters, peptide exporters, and systems that transport nonprotein substrates. Prototype exporters from each group are described in detail to illustrate our current understanding of this protein family. The prototype systems include the alpha-hemolysin, colicin V, and capsular polysaccharide exporters from Escherichia coli, the protease exporter from Erwinia chrysanthemi, and the glucan exporters from Agrobacterium tumefaciens and Rhizobium meliloti. Phylogenetic analysis of the ATP-binding domains from 29 bacterial ABC exporters indicates that the bacterial ABC exporters can be divided into two primary branches. One branch contains the transport systems where the ATP-binding domain and the membrane-spanning domain are present on the same polypeptide, and the other branch contains the systems where these domains are found on separate polypeptides. Differences in substrate specificity do not correlate with evolutionary relatedness. A complete survey of the known and putative bacterial ABC exporters is included at the end of the review.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/metabolism Biological Evolution Biological Transport Carrier Proteins/classification,physiology Gram-Negative Bacteria/physiology Gram-Positive Bacteria/physiology Molecular Sequence Data Polysaccharides, Bacterial/metabolism Sequence Homology, Amino Acid Substrate Specificity
Chemicals
Bacterial Proteins Carrier Proteins Polysaccharides, Bacterial
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fath M J
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115.
Kolter R
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Article Info
Journal
Microbiological reviews
Abbr.
Microbiol Rev
ISSN
0146-0749
DOI
10.1128/mr.57.4.995-1017.1993
Published
1993-12-00
Pages
995-1017
Language
English
Region
United States
NLM ID
7806086
PMCID
PMC372944
Subset
IM
Grants
NIAID NIH HHS · AI25944 · United States
External Links
PubMed source DOI: 10.1128/mr.57.4.995-1017.1993 PMC Full Text
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