Domain Shuffling During Evolution of the Proteins of the Bacterial Phosphotransferase System

Overview

Journal Res Microbiol

Publisher Elsevier

Specialty Microbiology

Date 1990 Nov 1

PMID 2092356

Citations 5

Authors

M H Saier Jr

J Reizer

Affiliations

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Abstract

About twenty permeases of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) have been sequenced and analysed. The results of these analyses suggest that interdomain shuffling, splicing, fusion, deletion, and duplication have occurred repeatedly during their evolution. A uniform nomenclature for these proteins and their domains is proposed.

Citing Articles

Functional and structural diversification of incomplete phosphotransferase system in cellulose-degrading clostridia.

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The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.

Deutscher J, Ake F, Derkaoui M, Zebre A, Cao T, Bouraoui H Microbiol Mol Biol Rev. 2014; 78(2):231-56.

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Computer-aided analyses of transport protein sequences: gleaning evidence concerning function, structure, biogenesis, and evolution.

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P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees.

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Evolutionary relationships among the permease proteins of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Construction of phylogenetic trees and possible relatedness to proteins of eukaryotic mitochondria.

Reizer A, Pao G, Saier Jr M J Mol Evol. 1991; 33(2):179-93.

PMID: 1920454 DOI: 10.1007/BF02193633.