| Range |
~35 %
|
| Organism |
Bacteria Escherichia coli |
| Reference |
De Geyter J et al., Protein folding in the cell envelope of Escherichia coli. Nat Microbiol. 2016 Jul 26 1(8):16107. doi: 10.1038/nmicrobiol.2016.107 p.1 left column 2nd paragraphPubMed ID27573113
|
| Primary Source |
[5] Orfanoudaki, G. & Economou, A. Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb). Mol. Cell Proteomics 13, 3674–3687 (2014) doi: 10.1074/mcp.O114.041137PubMed ID25210196
|
| Method |
Primary source abstract: "Here [investigators] present the STEP database (STEPdb) that contains a comprehensive characterization of subcellular localization and topology of the complete proteome of Escherichia coli." |
| Comments |
P.1 left column 2nd paragraph: "In bacteria, such as the Gram-negative E. coli K12 strain, a remarkable ∼35% of the proteome, which [investigators] term the ‘exportome’, is extracytoplasmic and folds in the cell envelope or beyond [primary source] (Fig. 1). The exportome comprises all proteins that reside in non-cytoplasmic compartments and mediates basic cell functions: cell shape and division, locomotion and adherence, DNA transfer, nutrient scavenging, decomposition and uptake of molecules, keeping out antibiotics and toxins, and signal transduction. Moreover, exported proteins are major pathogenicity determinants. These proteins must navigate the complex physiology of the Gram-negative envelope for correct placement, folding and function." |
| Entered by |
Uri M |
| ID |
114120 |