Tag | Content |
---|
CPLM ID | CPLM-003448 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Chemotaxis protein CheY |
Protein Synonyms/Alias | |
Gene Name | cheY |
Gene Synonyms/Alias | b1882; JW1871 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
---|
4 | ****MADKELKFLVV | acetylation | [1] | 7 | *MADKELKFLVVDDF | acetylation | [1, 2] | 26 | RIVRNLLKELGFNNV | acetylation | [1, 2] | 70 | MDGLELLKTIRADGA | acetylation | [1] | 91 | LMVTAEAKKENIIAA | acetylation | [1, 2] | 92 | MVTAEAKKENIIAAA | acetylation | [1, 2] | 109 | GASGYVVKPFTAATL | acetylation | [1, 2] | 119 | TAATLEEKLNKIFEK | acetylation | [1, 2] | 122 | TLEEKLNKIFEKLGM | acetylation | [1, 2] | 126 | KLNKIFEKLGM**** | acetylation | [2] |
|
Reference | [1] Acetylation represses the binding of CheY to its target proteins. Liarzi O, Barak R, Bronner V, Dines M, Sagi Y, Shainskaya A, Eisenbach M. Mol Microbiol. 2010 May;76(4):932-43. [ PMID: 20398208] [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 7 124 Response regulatory. METAL 12 12 Magnesium. METAL 13 13 Magnesium. METAL 57 57 Magnesium. METAL 59 59 Magnesium; via carbonyl oxygen. MOD_RES 57 57 4-aspartylphosphate. MOD_RES 92 92 N6-acetyllysine. MOD_RES 109 109 N6-acetyllysine. |
Keyword | 3D-structure; Acetylation; Chemotaxis; Complete proteome; Cytoplasm; Direct protein sequencing; Flagellar rotation; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Two-component regulatory system. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 129 AA |
Protein Sequence | MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG YGFVISDWNM 60 PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL 120 NKIFEKLGM 129 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0000287; F:magnesium ion binding; IMP:EcoCyc. GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro. GO:0006935; P:chemotaxis; IMP:EcoCyc. GO:0060286; P:flagellar cell motility; TAS:EcoCyc. GO:0035556; P:intracellular signal transduction; IEA:GOC. GO:0000160; P:phosphorelay signal transduction system; IDA:EcoCyc. GO:0006473; P:protein acetylation; IDA:EcoCyc. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |