Protein Variants | Comment | Organism |
---|---|---|
E268A | site-directed mutagenesis, in contrast to wild-type MurG, the MurG lipid interaction mutant often localizes to a single pole | Escherichia coli |
L79E/F82E | site-directed mutagenesis, the mutant does not bind anionic phospholipids but can localize to the cell poles | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | associated | Escherichia coli | 16020 | - |
additional information | MurG becomes polarly localized when expressed at high cellular concentrations, only at levels that saturate MurGs cellular requirement for growth, the polar MurG is not active | Escherichia coli | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
wild-type strain NCM3722 and diverse modified strains, gene murG | - |
Synonyms | Comment | Organism |
---|---|---|
MurG | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | MurG is an essential N-acetylglucosaminyl transferase involved in catalyzing the final step of peptidoglycan subunit biosynthesis | Escherichia coli |
additional information | MurG becomes polarly localized when expressed at high cellular concentrations, only at levels that saturate MurGs cellular requirement for growth, the polar MurG is not active and polar MurG is dynamic. It can be remobilized when MurG levels drop | Escherichia coli |
physiological function | MurG represents a temporary storage mechanism for excess protein that can later be remobilized into the active pool. Polar MurG can promote polar accumulation of anionic phospholipids | Escherichia coli |