UniProt functional annotation for P69783

UniProt codes: P69783, P08837.

Organism: Escherichia coli (strain K12).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
 
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:3129430, PubMed:17158705). The enzyme II complex composed of PtsG and Crr is involved in glucose transport (PubMed:2657735). The non-phosphorylated EIII-Glc is an inhibitor for uptake of certain sugars such as maltose, melibiose, lactose, and glycerol. Phosphorylated EIII-Glc, however, may be an activator for adenylate cyclase. It is an important regulatory protein for cell metabolism (PubMed:789369). {ECO:0000269|PubMed:2657735, ECO:0000269|PubMed:3129430, ECO:0000269|PubMed:789369, ECO:0000305|PubMed:17158705}.
 
Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:9405042}; Note=Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization. {ECO:0000269|PubMed:8170944};
Subunit: Heterodimer with glycerol kinase (glpk). {ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:8430315, ECO:0000305|PubMed:9405042}.
Subcellular location: Cytoplasm {ECO:0000305}.
Domain: The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain. {ECO:0000255|PROSITE-ProRule:PRU00416}.
Disruption phenotype: In mutants defective in enzyme I and histidine- containing phosphate carrier protein (HPr), cells lacking this gene are able to grow on the non-PTS compounds such as glycerol, maltose, melibiose, mannose 6-phosphate, and alpha-glycerol phosphate. {ECO:0000269|PubMed:789369}.

Annotations taken from UniProtKB at the EBI.