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UniProt functional annotation for P0AE67 | ||
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| UniProt code: P0AE67. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator. {ECO:0000269|PubMed:20346719}. |
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| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; |
| Subunit: | |
Interacts (phosphorylated CheY) with CheZ (via C-terminus). {ECO:0000269|PubMed:12080332, ECO:0000269|PubMed:9437425}. |
| Subcellular location: | |
Cytoplasm. |
| Ptm: | |
Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available. The major acetylation site seems to be Lys-92. Dephosphorylated (inactivated) by CheZ. {ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:1390767, ECO:0000269|PubMed:2689446, ECO:0000269|PubMed:3280143, ECO:0000269|PubMed:9560203}. |
| Mass spectrometry: | |
Mass=13966; Method=Electrospray; Evidence={ECO:0000269|PubMed:9560203}; |
| Mass spectrometry: | |
Mass=14008; Method=Electrospray; Note=With N6- acetyl-Lys-92.; Evidence={ECO:0000269|PubMed:9560203}; |
Annotations taken from UniProtKB at the EBI.