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UniProtKB/Swiss-Prot entry P07363


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CHEA_ECOLI
Primary accession number P07363
Secondary accession number P76302
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on November 1, 1997 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 103)
Name and origin of the protein
Protein name Chemotaxis protein cheA
Synonym EC 2.7.13.3
Gene name
Name: cheA
OrderedLocusNames: b1888, JW1877
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2002011 [NCBI, ExPASy, EBI, Israel, Japan]
Kofoid E.C., Parkinson J.S.;
"Tandem translation starts in the cheA locus of Escherichia coli.";
J. Bacteriol. 173:2116-2119(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh T., Aiba H., Baba T., Fujita K., 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., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.;
"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(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, 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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-654.
PubMed=3510184 [NCBI, ExPASy, EBI, Israel, Japan]
Mutoh N., Simon M.I.;
"Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli.";
J. Bacteriol. 165:161-166(1986).
[6]
PHOSPHORYLATION, AND DOMAINS.
DOI=10.1016/0092-8674(88)90490-4; PubMed=2832069 [NCBI, ExPASy, EBI, Israel, Japan]
Oosawa K., Hess J.F., Simon M.I.;
"Mutants defective in bacterial chemotaxis show modified protein phosphorylation.";
Cell 53:89-96(1988).
[7]
SUBUNIT.
PubMed=2068106 [NCBI, ExPASy, EBI, Israel, Japan]
McNally D.F., Matsumura P.;
"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(1991).
[8]
STRUCTURE BY NMR OF 1-233.
DOI=10.1021/bi951960e; PubMed=8555213 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou H., McEvoy M.M., Lowry D.F., Swanson R.V., Simon M.I., Dahlquist F.W.;
"Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker.";
Biochemistry 35:433-443(1996).
[9]
STRUCTURE BY NMR OF 124-257.
DOI=10.1021/bi952707h; PubMed=8639521 [NCBI, ExPASy, EBI, Israel, Japan]
McEvoy M.M., Muhandiram D.R., Kyw L.E., Dahlquist F.W.;
"Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy.";
Biochemistry 35:5633-5640(1996).
[10]
STRUCTURE BY NMR OF 1-134.
DOI=10.1021/bi961663p; PubMed=9020767 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou H., Dahlquist F.W.;
"Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.";
Biochemistry 36:699-710(1997).
[11]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 158-228.
DOI=10.1038/nsb0198-25; PubMed=9437425 [NCBI, ExPASy, EBI, Israel, Japan]
Welch M., Chinardet N., Mourey L., Birck C., Samama J.-P.;
"Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY.";
Nat. Struct. Biol. 5:25-29(1998).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 158-226.
DOI=10.1073/pnas.95.13.7333; PubMed=9636149 [NCBI, ExPASy, EBI, Israel, Japan]
McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., Dahlquist F.W.;
"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(1998).
Comments
  • 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.
  • CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
  • SUBUNIT: An in vitro complex of cheW/cheA(L)/cheA(S) in a 1:1:1 ratio increases the autophosphorylation of cheA and is required for the binding of cheY, the phosphorylation substrate. This complex accounts for 10% of the total number of molecules.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative initiation.
    NamecheA(L)
    Synonymslong, large
    Isoform IDP07363-1
    This is the isoform sequence displayed in this entry.
    NamecheA(S)
    Synonymsshort
    Isoform IDP07363-2
    Features which should be applied to build the isoform sequence: VSP_018886.
  • DOMAIN: May have three functional domains: one for interaction with cheB and cheY, a second for regulating phosphorylation and controlling the stability of the protein, and a third for receiving input signals regulating cheA activity.
  • SIMILARITY: Contains 1 cheW-like domain.
  • SIMILARITY: Contains 1 histidine kinase domain.
  • SIMILARITY: Contains 1 HPt domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M34669; AAA23573.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34669; AAA23574.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74958.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15709.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M13462; AAA23564.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H64951; QRECCS.
RefSeq AP_002508.1; -.
NP_416402.1; -.
3D structure databases
PDB
1A0O; X-ray; 2.95 A; B/D/F/H=124-257.[ExPASy / RCSB / EBI]
1EAY; X-ray; 2.00 A; C/D=156-228.[ExPASy / RCSB / EBI]
1FFG; X-ray; 2.10 A; B/D=124-257.[ExPASy / RCSB / EBI]
1FFS; X-ray; 2.40 A; B/D=124-257.[ExPASy / RCSB / EBI]
1FFW; X-ray; 2.70 A; A/C=1-3, B/D=124-257.[ExPASy / RCSB / EBI]
1FWP; NMR; -; A=124-257.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A0O; -.
1EAY; -.
1FFG; -.
1FFS; -.
1FFW; -.
1FWP; -.
SMR P07363; 4-131.
DisProt DP00407; -.
ModBase P07363.
Protein-protein interaction databases
DIP DIP:6053N; -.
Enzyme and pathway databases
BioCyc EcoCyc:CHEA-SMALL; -.
EcoCyc:PROTEIN-CHEA; -.
Organism-specific databases
EchoBASE EB0144; -.
EcoGene EG10146; cheA.
Family and domain databases
InterPro IPR003594; ATP_bd_ATPase.
IPR002545; CheW.
IPR015162; CheY-binding.
IPR004358; Sig_transdc_His_kin-like_C.
IPR008207; Sig_transdc_His_kin_P-trf.
IPR004105; Sig_transdc_His_kin_subgr_dim.
IPR005467; Sig_transdc_His_kinase_core.
Graphical view of domain structure.
Gene3D G3DSA:3.30.565.10; ATP_bd_ATPase; 1.
Pfam PF01584; CheW; 1.
PF09078; CheY-binding; 1.
PF02895; H-kinase_dim; 1.
PF02518; HATPase_c; 1.
PF01627; Hpt; 1.
Pfam graphical view of domain structure.
PRINTS PR00344; BCTRLSENSOR.
ProDom PD003142; Hpt_N; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00260; CheW; 1.
SM00387; HATPase_c; 1.
SM00073; HPT; 1.
SMART graphical view of domain structure.
PROSITE PS50851; CHEW; 1.
PS50109; HIS_KIN; 1.
PS50894; HPT; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P07363.
ProtoNet P07363.
Genome annotation databases
GeneID 946401; -.
GenomeReviews U00096_GR; b1888.
AP009048_GR; JW1877.
KEGG ecj:JW1877; -.
eco:b1888; -.
Phylogenomic databases
HOGENOM P07363; -.
Other
LinkHub P07363; -.
Genome annotation databases
CMR P07363; b1888.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative initiation; Chemotaxis; Complete proteome; Cytoplasm; Kinase; Phosphoprotein; Transferase; Two-component regulatory system.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   654  654     Chemotaxis protein cheA. PRO_0000032373
DOMAIN   1   105  105     HPt. 
DOMAIN   257   509  253     Histidine kinase. 
DOMAIN   511   646  136     CheW-like. 
MOD_RES   48    48        Phosphohistidine; by autocatalysis. 
VAR_SEQ   1    97        Missing (in isoform cheA(S)). VSP_018886
CONFLICT   166   166        R -> P (in Ref. 1; AAA23573/AAA23574). 
CONFLICT   548   565        GERVLEVRGEYLPIVELW -> ASGCWKCGVNICPSSNCG (in Ref. 5; AAA23564). 
CONFLICT   606   606        V -> A (in Ref. 5; AAA23564). 
STRAND   161   164  4      
HELIX   171   182  12      
STRAND   186   190  5      
STRAND   195   198  4      
HELIX   205   212  8      
TURN   213   215  3      
STRAND   220   224  5      
Sequence information
Length: 654 AA [This is the length of the unprocessed precursor] Molecular weight: 71382 Da [This is the MW of the unprocessed precursor] CRC64: 009B824154E269B4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSMDISDFYQ TFFDEADELL ADMEQHLLVL QPEAPDAEQL NAIFRAAHSI KGGAGTFGFS 

        70         80         90        100        110        120 
VLQETTHLME NLLDEARRGE MQLNTDIINL FLETKDIMQE QLDAYKQSQE PDAASFDYIC 

       130        140        150        160        170        180 
QALRQLALEA KGETPSAVTR LSVVAKSEPQ DEQSRSQSPR RIILSRLKAG EVDLLEEELG 

       190        200        210        220        230        240 
HLTTLTDVVK GADSLSAILP GDIAEDDITA VLCFVIEADQ ITFETVEVSP KISTPPVLKL 

       250        260        270        280        290        300 
AAEQAPTGRV EREKTTRSNE STSIRVAVEK VDQLINLVGE LVITQSMLAQ RSSELDPVNH 

       310        320        330        340        350        360 
GDLITSMGQL QRNARDLQES VMSIRMMPME YVFSRYPRLV RDLAGKLGKQ VELTLVGSST 

       370        380        390        400        410        420 
ELDKSLIERI IDPLTHLVRN SLDHGIELPE KRLAAGKNSV GNLILSAEHQ GGNICIEVTD 

       430        440        450        460        470        480 
DGAGLNRERI LAKAASQGLT VSENMSDDEV AMLIFAPGFS TAEQVTDVSG RGVGMDVVKR 

       490        500        510        520        530        540 
NIQKMGGHVE IQSKQGTGTT IRILLPLTLA ILDGMSVRVA DEVFILPLNA VMESLQPREA 

       550        560        570        580        590        600 
DLHPLAGGER VLEVRGEYLP IVELWKVFNV AGAKTEATQG IVVILQSGGR RYALLVDQLI 

       610        620        630        640        650 
GQHQVVVKNL ESNYRKVPGI SAATILGDGS VALIVDVSAL QAINREQRMA NTAA 

P07363 in FASTA format

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View entry in raw text format (no links)
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