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P07363 (CHEA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chemotaxis protein CheA

EC=2.7.13.3
Gene names
Name:cheA
Ordered Locus Names:b1888, JW1877
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 structure

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. Ref.7

Subcellular location

Cytoplasm.

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. Ref.6

Sequence similarities

Contains 1 cheW-like domain.

Contains 1 histidine kinase domain.

Contains 1 HPt domain.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform cheA(L) (identifier: P07363-1)

Also known as: long; large;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform cheA(S) (identifier: P07363-2)

Also known as: short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 654654Chemotaxis protein CheA
PRO_0000032373

Regions

Domain1 – 105105HPt
Domain257 – 509253Histidine kinase
Domain511 – 646136CheW-like

Amino acid modifications

Modified residue481Phosphohistidine; by autocatalysis

Natural variations

Alternative sequence1 – 9797Missing in isoform cheA(S).
VSP_018886

Experimental info

Sequence conflict1661R → P in AAA23573. Ref.1
Sequence conflict1661R → P in AAA23574. Ref.1
Sequence conflict548 – 56518GERVL…IVELW → ASGCWKCGVNICPSSNCG in AAA23564. Ref.5
Sequence conflict6061V → A in AAA23564. Ref.5

Secondary structure

............................... 654
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform cheA(L) (long) (large) [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 009B824154E269B4

FASTA65471,382
        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 

« Hide

Isoform cheA(S) (short) [UniParc].

Checksum: 8982A8C04F2AEDBA
Show »

FASTA55760,422

References

« Hide 'large scale' references
[1]"Tandem translation starts in the cheA locus of Escherichia coli."
Kofoid E.C., Parkinson J.S.
J. Bacteriol. 173:2116-2119(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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."
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. expand/collapse author list , 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.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli."
Mutoh N., Simon M.I.
J. Bacteriol. 165:161-166(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-654.
[6]"Mutants defective in bacterial chemotaxis show modified protein phosphorylation."
Oosawa K., Hess J.F., Simon M.I.
Cell 53:89-96(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DOMAINS.
[7]"Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex enhances autophosphorylation and affinity for CheY."
McNally D.F., Matsumura P.
Proc. Natl. Acad. Sci. U.S.A. 88:6269-6273(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[8]"Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker."
Zhou H., McEvoy M.M., Lowry D.F., Swanson R.V., Simon M.I., Dahlquist F.W.
Biochemistry 35:433-443(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-233.
[9]"Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy."
McEvoy M.M., Muhandiram D.R., Kyw L.E., Dahlquist F.W.
Biochemistry 35:5633-5640(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 124-257.
[10]"Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR."
Zhou H., Dahlquist F.W.
Biochemistry 36:699-710(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-134.
[11]"Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY."
Welch M., Chinardet N., Mourey L., Birck C., Samama J.-P.
Nat. Struct. Biol. 5:25-29(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 158-228.
[12]"Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway."
McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., Dahlquist F.W.
Proc. Natl. Acad. Sci. U.S.A. 95:7333-7338(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 158-226.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34669 Genomic DNA. Translation: AAA23573.1.
M34669 Genomic DNA. Translation: AAA23574.1.
U00096 Genomic DNA. Translation: AAC74958.1.
AP009048 Genomic DNA. Translation: BAA15709.1.
M13462 Genomic DNA. Translation: AAA23564.1.
PIRQRECCS. H64951.
RefSeqNP_416402.1. NC_000913.3.
YP_490150.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0OX-ray2.95B/D/F/H124-257[»]
1EAYX-ray2.00C/D156-228[»]
1FFGX-ray2.10B/D124-257[»]
1FFSX-ray2.40B/D124-257[»]
1FFWX-ray2.70B/D124-257[»]
1FWPNMR-A124-257[»]
2LP4NMR-A1-225[»]
DisProtDP00407.
ProteinModelPortalP07363.
SMRP07363. Positions 1-226, 261-640.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6053N.
IntActP07363. 33 interactions.
MINTMINT-1312842.
STRING511145.b1888.

Proteomic databases

PaxDbP07363.
PRIDEP07363.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74958; AAC74958; b1888.
BAA15709; BAA15709; BAA15709.
GeneID12932040.
946401.
KEGGecj:Y75_p1864.
eco:b1888.
PATRIC32119103. VBIEscCol129921_1969.

Organism-specific databases

EchoBASEEB0144.
EcoGeneEG10146. cheA.

Phylogenomic databases

eggNOGCOG0643.
HOGENOMHOG000255263.
KOK03407.
OMAKISTPPM.
OrthoDBEOG62RS8P.
PhylomeDBP07363.
ProtClustDBPRK10547.

Enzyme and pathway databases

BioCycEcoCyc:CHEA-SMALL.
EcoCyc:PROTEIN-CHEA.
ECOL316407:JW1877-MONOMER.
BRENDA2.7.13.3. 2026.

Gene expression databases

GenevestigatorP07363.

Family and domain databases

Gene3D1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.400. 1 hit.
InterProIPR004105. CheA-like_dim.
IPR002545. CheW.
IPR015162. CheY-binding.
IPR003594. HATPase_ATP-bd.
IPR004358. Sig_transdc_His_kin-like_C.
IPR008207. Sig_transdc_His_kin_Hpt_dom.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
[Graphical view]
PfamPF01584. CheW. 1 hit.
PF09078. CheY-binding. 1 hit.
PF02895. H-kinase_dim. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01627. Hpt. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00260. CheW. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view]
SUPFAMSSF47226. SSF47226. 1 hit.
SSF47384. SSF47384. 1 hit.
SSF50341. SSF50341. 1 hit.
SSF55052. SSF55052. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEPS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07363.
PROP07363.

Entry information

Entry nameCHEA_ECOLI
AccessionPrimary (citable) accession number: P07363
Secondary accession number(s): P76302
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene