Molecular analysis of the Escherichia coli K5 kps locus: identification and characterization of an inner-membrane capsular polysaccharide transport system
| Autor: | Annabel Smith, I S Roberts, Graham J. Boulnois |
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| Rok vydání: | 1990 |
| Předmět: |
Protein Conformation
Molecular Sequence Data Restriction Mapping Biology medicine.disease_cause Microbiology Protein structure Bacterial Proteins Sequence Homology Nucleic Acid Escherichia coli medicine Inner membrane Amino Acid Sequence Molecular Biology Peptide sequence Capsular polysaccharide transport Base Sequence Membrane transport protein Escherichia coli Proteins Cell Membrane Polysaccharides Bacterial Nucleic acid sequence Membrane Transport Proteins Nucleic Acid Hybridization Periplasmic space Biochemistry Genes Bacterial Multigene Family biology.protein ATP-Binding Cassette Transporters |
| Zdroj: | Molecular Microbiology. 4:1863-1869 |
| ISSN: | 1365-2958 0950-382X |
| DOI: | 10.1111/j.1365-2958.1990.tb02035.x |
| Popis: | The complete nucleotide sequence has been determined of a region of the Escherichia coli K5 antigen gene cluster postulated to encode functions for the translocation of capsular polysaccharide across the inner membrane. This revealed two genes, designated kpsM and kpsT, organized in a single transcriptional unit. Analysis of the predicted amino acid sequence of the KpsM and KpsT proteins indicates that they may function as dual components in a polysaccharide export system analogous to the periplasmic binding protein-dependent transport systems of Gram-negative bacteria. We propose that the KpsT protein acts as an energizer, coupling ATP hydrolysis to the transport process mediated by the KpsM protein. Extensive sequence homology between the KpsM and KpsT proteins and the products of the bexB and bexA genes present in the capsulation (cap) locus of Haemophilus influenzae, indicates that a common mechanism for the export of polysaccharide across the inner membrane may exist in these two micro-organisms. |
| Databáze: | OpenAIRE |
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