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P07363

- CHEA_ECOLI

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Protein
Chemotaxis protein CheA
Gene
cheA, b1888, JW1877

Gene:

cheA, b1888, JW1877
Organism
Escherichia coli (strain K12)
Status
Reviewed - - Experimental evidence at protein leveli

UniProt

P07363 - CHEA_ECOLI

Protein:

Chemotaxis protein CheA
Protein Existence: Experimental evidence at protein level

Functioni

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 activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

GO - Molecular functioni

  1. ATP bindingInferred from electronic annotationi Source: UniProtKB-KW
  2. phosphorelay sensor kinase activityInferred from electronic annotationi Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. ATP bindingInferred from electronic annotationi Source: UniProtKB-KW
  2. phosphorelay sensor kinase activityInferred from electronic annotationi Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Chemotaxis, Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CHEA-SMALL.
EcoCyc:PROTEIN-CHEA.
ECOL316407:JW1877-MONOMER.
BRENDAi2.7.13.3. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheA (EC:2.7.13.3)
Gene namesi
Name:cheA
Ordered Locus Names:b1888, JW1877
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10146. cheA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmInferred from electronic annotationi Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Chaini1 – 654654Chemotaxis protein CheA
PRO_0000032373

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Modified residuei481Phosphohistidine; by autocatalysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP07363.
PRIDEiP07363.

Expressioni

Gene expression databases

GenevestigatoriP07363.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
cheYP0AE673EBI-1026773,EBI-546693
cheZP0A9H93EBI-1026773,EBI-546726

Protein-protein interaction databases

DIPiDIP-6053N.
IntActiP07363. 33 interactions.
MINTiMINT-1312842.
STRINGi511145.b1888.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Helixi5 – 73
Helixi9 – 2921
Helixi37 – 5620
Helixi60 – 7718
Helixi85 – 10622
Helixi113 – 13018
Beta strandi140 – 1456
Beta strandi151 – 1544
Beta strandi161 – 1644
Helixi171 – 18212
Beta strandi186 – 1905
Beta strandi195 – 1984
Beta strandi201 – 2044
Helixi205 – 2128
Turni213 – 2153
Beta strandi220 – 2245

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00407.
ProteinModelPortaliP07363.
SMRiP07363. Positions 1-226, 261-640.

Miscellaneous databases

EvolutionaryTraceiP07363.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Domaini1 – 105105HPt
Domaini257 – 509253Histidine kinase
Domaini511 – 646136CheW-like

Domaini

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.1 Publication

Sequence similaritiesi

Contains 1 cheW-like domain.
Contains 1 HPt domain.

Phylogenomic databases

eggNOGiCOG0643.
HOGENOMiHOG000255263.
KOiK03407.
OMAiKISTPPM.
OrthoDBiEOG62RS8P.
ProtClustDBiPRK10547.

Family and domain databases

Gene3Di1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.400. 1 hit.
InterProiIPR004105. 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]
PfamiPF01584. 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]
PRINTSiPR00344. BCTRLSENSOR.
SMARTiSM00260. CheW. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view]
SUPFAMiSSF47226. SSF47226. 1 hit.
SSF47384. SSF47384. 1 hit.
SSF50341. SSF50341. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform cheA(L) (identifier: P07363-1) [UniParc]FASTA

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.

« Hide

MSMDISDFYQ TFFDEADELL ADMEQHLLVL QPEAPDAEQL NAIFRAAHSI    50
KGGAGTFGFS VLQETTHLME NLLDEARRGE MQLNTDIINL FLETKDIMQE 100
QLDAYKQSQE PDAASFDYIC QALRQLALEA KGETPSAVTR LSVVAKSEPQ 150
DEQSRSQSPR RIILSRLKAG EVDLLEEELG HLTTLTDVVK GADSLSAILP 200
GDIAEDDITA VLCFVIEADQ ITFETVEVSP KISTPPVLKL AAEQAPTGRV 250
EREKTTRSNE STSIRVAVEK VDQLINLVGE LVITQSMLAQ RSSELDPVNH 300
GDLITSMGQL QRNARDLQES VMSIRMMPME YVFSRYPRLV RDLAGKLGKQ 350
VELTLVGSST ELDKSLIERI IDPLTHLVRN SLDHGIELPE KRLAAGKNSV 400
GNLILSAEHQ GGNICIEVTD DGAGLNRERI LAKAASQGLT VSENMSDDEV 450
AMLIFAPGFS TAEQVTDVSG RGVGMDVVKR NIQKMGGHVE IQSKQGTGTT 500
IRILLPLTLA ILDGMSVRVA DEVFILPLNA VMESLQPREA DLHPLAGGER 550
VLEVRGEYLP IVELWKVFNV AGAKTEATQG IVVILQSGGR RYALLVDQLI 600
GQHQVVVKNL ESNYRKVPGI SAATILGDGS VALIVDVSAL QAINREQRMA 650
NTAA 654
Length:654
Mass (Da):71,382
Last modified:November 1, 1997 - v3
Checksum:i009B824154E269B4
GO
Isoform cheA(S) (identifier: P07363-2) [UniParc]FASTA

Also known as: short

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

Show »
Length:557
Mass (Da):60,422
Checksum:i8982A8C04F2AEDBA
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Alternative sequencei1 – 9797Missing in isoform cheA(S).
VSP_018886

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflicti1661R → P in AAA23573. 1 Publication
Sequence conflicti1661R → P in AAA23574. 1 Publication
Sequence conflicti548 – 56518GERVL…IVELW → ASGCWKCGVNICPSSNCG in AAA23564. 1 Publication
Sequence conflicti6061V → A in AAA23564. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiQRECCS. H64951.
RefSeqiNP_416402.1. NC_000913.3.
YP_490150.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74958; AAC74958; b1888.
BAA15709; BAA15709; BAA15709.
GeneIDi12932040.
946401.
KEGGiecj:Y75_p1864.
eco:b1888.
PATRICi32119103. VBIEscCol129921_1969.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi QRECCS. H64951.
RefSeqi NP_416402.1. NC_000913.3.
YP_490150.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A0O X-ray 2.95 B/D/F/H 124-257 [» ]
1EAY X-ray 2.00 C/D 156-228 [» ]
1FFG X-ray 2.10 B/D 124-257 [» ]
1FFS X-ray 2.40 B/D 124-257 [» ]
1FFW X-ray 2.70 B/D 124-257 [» ]
1FWP NMR - A 124-257 [» ]
2LP4 NMR - A 1-225 [» ]
DisProti DP00407.
ProteinModelPortali P07363.
SMRi P07363. Positions 1-226, 261-640.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-6053N.
IntActi P07363. 33 interactions.
MINTi MINT-1312842.
STRINGi 511145.b1888.

Proteomic databases

PaxDbi P07363.
PRIDEi P07363.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74958 ; AAC74958 ; b1888 .
BAA15709 ; BAA15709 ; BAA15709 .
GeneIDi 12932040.
946401.
KEGGi ecj:Y75_p1864.
eco:b1888.
PATRICi 32119103. VBIEscCol129921_1969.

Organism-specific databases

EchoBASEi EB0144.
EcoGenei EG10146. cheA.

Phylogenomic databases

eggNOGi COG0643.
HOGENOMi HOG000255263.
KOi K03407.
OMAi KISTPPM.
OrthoDBi EOG62RS8P.
ProtClustDBi PRK10547.

Enzyme and pathway databases

BioCyci EcoCyc:CHEA-SMALL.
EcoCyc:PROTEIN-CHEA.
ECOL316407:JW1877-MONOMER.
BRENDAi 2.7.13.3. 2026.

Miscellaneous databases

EvolutionaryTracei P07363.
PROi P07363.

Gene expression databases

Genevestigatori P07363.

Family and domain databases

Gene3Di 1.10.287.560. 1 hit.
1.20.120.160. 1 hit.
3.30.565.10. 1 hit.
3.30.70.400. 1 hit.
InterProi IPR004105. 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 ]
Pfami PF01584. 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 ]
PRINTSi PR00344. BCTRLSENSOR.
SMARTi SM00260. CheW. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00073. HPT. 1 hit.
[Graphical view ]
SUPFAMi SSF47226. SSF47226. 1 hit.
SSF47384. SSF47384. 1 hit.
SSF50341. SSF50341. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEi PS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  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.
    , 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.

Entry nameiCHEA_ECOLI
AccessioniPrimary (citable) accession number: P07363
Secondary accession number(s): P76302
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

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