CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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****MADKELKFLVVacetylation[1]
7*MADKELKFLVVDDFacetylation[1, 2]
26RIVRNLLKELGFNNVacetylation[1, 2]
70MDGLELLKTIRADGAacetylation[1]
91LMVTAEAKKENIIAAacetylation[1, 2]
92MVTAEAKKENIIAAAacetylation[1, 2]
109GASGYVVKPFTAATLacetylation[1, 2]
119TAATLEEKLNKIFEKacetylation[1, 2]
122TLEEKLNKIFEKLGMacetylation[1, 2]
126KLNKIFEKLGM****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
 IPR011006; CheY-like_superfamily.
 IPR001789; Sig_transdc_resp-reg_receiver. 
Pfam
 PF00072; Response_reg 
SMART
 SM00448; REC 
PROSITE
 PS50110; RESPONSE_REGULATORY 
PRINTS