Novel Phosphotransferase System Genes Revealed by Bacterial Genome Analysis: The Complete Complement of pts Genes in Mycoplasma genitalium
| Autor: | Friedrich Titgemeyer, Aiala Reizer, Ian T. Paulsen, Milton H. Saier, Jonathan Reizer |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Genetics
biology Phosphotransferases (Nitrogenous Group Acceptor) Chromosome Sequence Analysis DNA PEP group translocation Bacterial genome size bacterial infections and mycoses urologic and male genital diseases biology.organism_classification female genital diseases and pregnancy complications Evolution Molecular Complete sequence Mycoplasma Bacterial Proteins Genes Bacterial Multigene Family Phosphoenolpyruvate Sugar Phosphotransferase System Mycoplasma genitalium Gene Genome Bacterial Phylogeny |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1070-2830 |
| DOI: | 10.1089/mcg.1996.1.151 |
| Popis: | The complete sequence of the Mycoplasma genitalium chromosome has recently been determined. We here report analyses of the genes encoding proteins of the phosphoenolpyruvate:sugar phosphotransferase system, PTS. These genes encode (1) Enzyme I, (2) HPr, (3) a glucose-specific Enzyme IICBA, (4) an inactive glucose-specific Enzyme IIB, lacking the active site cysteyl residue, and (5) a fructose-specific Enzyme IIABC. Some of the unique features of these genes and their enzyme products are as follows. (1) Each of the genes is encoded within a distinct operon. (2) Both Enzyme I and HPr have basic isoelectric points. (3) The glucose-specific Enzyme IIC bears a centrally located, hydrophilic, 200 amino acyl residue insert that lacks sequence similarity with any protein in the current database. (4) The fructose-specific Enzyme II has a domain order (IIABC), different from those of previously characterized fructose permeases, and its IIA domain more closely resembles the IIANtr protein of Escherichia coli than other fructose-specific IIA domains. The potential significance of these novel features is discussed. |
| Databáze: | OpenAIRE |
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