Chemotaxis protein CheA (P07363)

Identification
Name:Chemotaxis protein CheA
Synonyms:Not Available
Gene Name:cheA
Enzyme Class:
Biological Properties
General Function:Cell motility
Specific Function:Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
kinase activity
molecular transducer activity
nucleoside binding
protein histidine kinase activity
protein kinase activity
purine nucleoside binding
signal transducer activity
transferase activity
transferase activity, transferring phosphorus-containing groups
two-component sensor activity
Process
biological regulation
cellular metabolic process
chemotaxis
metabolic process
peptidyl-histidine phosphorylation
phosphate metabolic process
phosphorus metabolic process
phosphorylation
protein amino acid phosphorylation
regulation of biological process
regulation of cellular process
response to chemical stimulus
response to stimulus
signal transduction
signal transmission
signaling process
two-component signal transduction system (phosphorelay)
Gene Properties
Blattner:Not Available
Gene OrientationNot Available
Centisome Percentage:Not Available
Left Sequence EndNot Available
Right Sequence EndNot Available
Gene Sequence:
>1965 bp
GTGAGCATGGATATAAGCGATTTTTATCAGACATTTTTTGATGAAGCGGACGAACTGTTG
GCTGACATGGAGCAGCATTTGCTGGTTTTGCAGCCGGAAGCGCCAGATGCCGAACAATTG
AATGCCATCTTTCGGGCTGCCCACTCGATCAAAGGAGGGGCAGGAACTTTTGGCTTCAGC
GTTTTGCAGGAAACCACGCATCTGATGGAAAACCTGCTCGATGAAGCCAGACGAGGTGAG
ATGCAACTCAACACCGACATTATCAATCTGTTTTTGGAAACGAAGGACATCATGCAAGAA
CAGCTCGACGCTTATAAACAGTCGCAAGAGCCGGATGCCGCCAGCTTCGATTATATCTGC
CAGGCCTTGCGTCAACTGGCATTAGAAGCGAAAGGCGAAACGCCATCCGCAGTGACCCGA
TTAAGTGTGGTTGCCAAAAGTGAACCGCAAGATGAGCAGAGTCGCAGTCAGTCGCCGCGA
CGAATTATCCTTTCGCCGCTGAAGGCCGGGGAAGTCGACCTGCTGGAAGAAGAACTGGGA
CATCTGACAACGTTAACTGACGTGGTGAAAGGGGCGGATTCGCTCTCGGCAATATTACCG
GGCGACATCGCCGAAGATGACATCACAGCGGTACTCTGTTTTGTGATTGAAGCCGATCAG
ATTACCTTTGAAACAGTAGAAGTCTCGCCAAAAATATCCACCCCACCAGTGCTTAAACTG
GCAGCCGAACAAGCGCCAACCGGCCGCGTGGAGCGGGAAAAAACGACGCGCAGCAATGAA
TCCACCAGCATCCGTGTAGCGGTAGAAAAGGTTGATCAATTAATTAACCTCGTCGGCGAG
CTGGTTATCACCCAGTCCATGCTTGCCCAGCGTTCCAGCGAACTGGACCCGGTTAATCAT
GGTGATTTGATAACCAGCATGGGGCAGTTACAACGTAACGCCCGTGATTTGCAGGAATCA
GTGATGTCGATTCGCATGATGCCGATGGAATATGTTTTTAGTCGCTATCCCCGGCTGGTG
CGTGATCTGGCGGGAAAACTCGGCAAGCAGGTAGAACTGACGCTGGTGGGCAGTTCTACT
GAACTCGACAAAAGCCTGATAGAACGCATTATCGACCCGCTGACCCACCTGGTACGCAAT
AGCCTCGATCACGGTATTGAACTGCCAGAAAAACGGCTCGCCGCAGGTAAAAACAGCGTC
GGAAATTTAATTCTGTCTGCCGAACATCAGGGCGGCAACATTTGCATTGAAGTGACCGAC
GATGGGGCGGGGCTAAACCGTGAGCGAATTCTGGCAAAAGCGGCCTCGCAAGGTTTGACT
GTCAGCGAAAACATGAGCGACGACGAAGTCGCGATGCTGATATTTGCACCTGGCTTCTCC
ACGGCAGAGCAGGTCACCGACGTCTCCGGGCGCGGCGTCGGCATGGACGTCGTTAAACGT
AATATCCAGAAGATGGGCGGTCATGTCGAAATCCAGTCGAAGCAGGGTACTGGCACTACG
ATCCGCATTTTACTGCCGCTGACGCTGGCCATCCTCGACGGCATGTCCGTACGCGTTGCG
GATGAAGTTTTCATTCTGCCGCTGAATGCTGTTATGGAATCACTGCAACCCCGTGAAGCC
GATCTCCATCCACTGGCCGGCGGCGAGCGGGTGCTGGAAGTGCGGGGTGAATATCTGCCC
ATCGTCGAACTGTGGAAAGTGTTCAACGTCGCGGGCGCGAAAACCGAAGCCACCCAGGGA
ATTGTGGTGATCTTACAAAGTGGCGGTCGCCGCTACGCCTTGCTGGTGGATCAATTAATT
GGTCAACACCAGGTTGTGGTTAAAAACCTTGAAAGTAACTATCGCAAAGTCCCCGGCATT
TCTGCTGCGACCATTCTTGGCGACGGCAGCGTGGCACTGATTGTTGATGTCTCCGCCTTG
CAGGCGATAAACCGCGAACAACGTATGGCGAACACCGCCGCCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:654
Protein Molecular Weight:71382
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Chemotaxis protein CheA
MSMDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFS
VLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMQEQLDAYKQSQEPDAASFDYIC
QALRQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELG
HLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKL
AAEQAPTGRVEREKTTRSNESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNH
GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSST
ELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTD
DGAGLNRERILAKAASQGLTVSENMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVKR
NIQKMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREA
DLHPLAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLI
GQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSALQAINREQRMANTAA
References
External Links:
ResourceLink
Uniprot ID:P07363
Uniprot Name:CHEA_ECOLI
GenBank Gene ID:M34669
Genebank Protein ID:145529
CCDB:CHEA_ECOLI
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Kofoid, E. C., Parkinson, J. S. (1991). "Tandem translation starts in the cheA locus of Escherichia coli." J Bacteriol 173:2116-2119. Pubmed: 2002011
  • McEvoy, M. M., Hausrath, A. C., Randolph, G. B., Remington, S. J., Dahlquist, F. W. (1998). "Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway." Proc Natl Acad Sci U S A 95:7333-7338. Pubmed: 9636149
  • McEvoy, M. M., Muhandiram, D. R., Kay, L. E., Dahlquist, F. W. (1996). "Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy." Biochemistry 35:5633-5640. Pubmed: 8639521
  • McNally, D. F., Matsumura, P. (1991). "Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex enhances autophosphorylation and affinity for CheY." Proc Natl Acad Sci U S A 88:6269-6273. Pubmed: 2068106
  • Mutoh, N., Simon, M. I. (1986). "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli." J Bacteriol 165:161-166. Pubmed: 3510184
  • Oosawa, K., Hess, J. F., Simon, M. I. (1988). "Mutants defective in bacterial chemotaxis show modified protein phosphorylation." Cell 53:89-96. Pubmed: 2832069
  • Welch, M., Chinardet, N., Mourey, L., Birck, C., Samama, J. P. (1998). "Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY." Nat Struct Biol 5:25-29. Pubmed: 9437425
  • Zhou, H., Dahlquist, F. W. (1997). "Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR." Biochemistry 36:699-710. Pubmed: 9020767
  • Zhou, H., McEvoy, M. M., Lowry, D. F., Swanson, R. V., Simon, M. I., Dahlquist, F. W. (1996). "Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker." Biochemistry 35:433-443. Pubmed: 8555213