IED ID |
IndEnz0002016718 |
Enzyme Type ID |
protease016718 |
Protein Name |
Chemotaxis protein CheY
|
Gene Name |
cheY |
Organism |
Yersinia enterocolitica |
Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Yersiniaceae
Yersinia
Yersinia enterocolitica
|
Enzyme Sequence |
MADKNLRFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLRTGGFDFVVSDWNMPNMDGLDLLKTIRADGALGTLPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM |
Enzyme Length |
129 |
Uniprot Accession Number |
Q93P00 |
Absorption |
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Active Site |
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Activity Regulation |
|
Binding Site |
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Calcium Binding |
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catalytic Activity |
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DNA Binding |
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EC Number |
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Enzyme Function |
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 (By similarity). {ECO:0000250}. |
Temperature Dependency |
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PH Dependency |
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Pathway |
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nucleotide Binding |
|
Features |
Chain (1); Domain (1); Initiator methionine (1); Metal binding (4); Modified residue (3) |
Keywords |
Acetylation;Chemotaxis;Cytoplasm;Flagellar rotation;Magnesium;Metal-binding;Phosphoprotein;Two-component regulatory system |
Interact With |
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Induction |
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Subcellular Location |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
Modified Residue |
MOD_RES 57; /note=4-aspartylphosphate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00169; MOD_RES 92; /note=N6-acetyllysine; /evidence=ECO:0000250; MOD_RES 109; /note=N6-acetyllysine; /evidence=ECO:0000250 |
Post Translational Modification |
PTM: Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available. {ECO:0000250}. |
Signal Peptide |
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Structure 3D |
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Cross Reference PDB |
- |
Mapped Pubmed ID |
- |
Motif |
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Gene Encoded By |
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Mass |
14,164 |
Kinetics |
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Metal Binding |
METAL 12; /note=Magnesium; /evidence=ECO:0000250; METAL 13; /note=Magnesium; /evidence=ECO:0000250; METAL 57; /note=Magnesium; /evidence=ECO:0000250; METAL 59; /note=Magnesium; via carbonyl oxygen; /evidence=ECO:0000250 |
Rhea ID |
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Cross Reference Brenda |
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