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Protein

Chemotaxis protein CheA

Gene

cheA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • chemotaxis Source: EcoCyc
  • establishment of localization in cell Source: EcoCyc
  • negative regulation of protein modification process Source: CACAO
  • phosphorelay signal transduction system Source: EcoliWiki
  • phosphorylation Source: EcoliWiki
  • positive regulation of protein dephosphorylation Source: EcoCyc
  • protein autophosphorylation Source: EcoliWiki
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.
RETL1328306-WGS:GSTH-3589-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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10146. cheA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
  • cytosol Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Chemotaxis protein CheAPRO_0000032373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphohistidine; by autocatalysisPROSITE-ProRule annotation1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP07363.
PRIDEiP07363.

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

1
654
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Helixi9 – 2921Combined sources
Helixi37 – 5620Combined sources
Helixi60 – 7718Combined sources
Helixi85 – 10622Combined sources
Helixi113 – 13018Combined sources
Beta strandi140 – 1456Combined sources
Beta strandi151 – 1544Combined sources
Beta strandi161 – 1644Combined sources
Helixi171 – 18212Combined sources
Beta strandi186 – 1905Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi201 – 2044Combined sources
Helixi205 – 2128Combined sources
Turni213 – 2153Combined sources
Beta strandi220 – 2245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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-A124-262[»]
2LP4NMR-A1-225[»]
DisProtiDP00407.
ProteinModelPortaliP07363.
SMRiP07363. Positions 1-226, 261-640.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07363.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 105105HPtPROSITE-ProRule annotationAdd
BLAST
Domaini257 – 509253Histidine kinasePROSITE-ProRule annotationAdd
BLAST
Domaini511 – 646136CheW-likePROSITE-ProRule annotationAdd
BLAST

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.PROSITE-ProRule annotation
Contains 1 histidine kinase domain.PROSITE-ProRule annotation
Contains 1 HPt domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0643.
HOGENOMiHOG000255263.
InParanoidiP07363.
KOiK03407.
OMAiVQTIRVN.
OrthoDBiEOG62RS8P.
PhylomeDBiP07363.

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_C.
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.
SSF55052. SSF55052. 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. AlignAdd to basket

Isoform cheA(L) (identifier: P07363-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MSMDISDFYQ TFFDEADELL ADMEQHLLVL QPEAPDAEQL NAIFRAAHSI
60 70 80 90 100
KGGAGTFGFS VLQETTHLME NLLDEARRGE MQLNTDIINL FLETKDIMQE
110 120 130 140 150
QLDAYKQSQE PDAASFDYIC QALRQLALEA KGETPSAVTR LSVVAKSEPQ
160 170 180 190 200
DEQSRSQSPR RIILSRLKAG EVDLLEEELG HLTTLTDVVK GADSLSAILP
210 220 230 240 250
GDIAEDDITA VLCFVIEADQ ITFETVEVSP KISTPPVLKL AAEQAPTGRV
260 270 280 290 300
EREKTTRSNE STSIRVAVEK VDQLINLVGE LVITQSMLAQ RSSELDPVNH
310 320 330 340 350
GDLITSMGQL QRNARDLQES VMSIRMMPME YVFSRYPRLV RDLAGKLGKQ
360 370 380 390 400
VELTLVGSST ELDKSLIERI IDPLTHLVRN SLDHGIELPE KRLAAGKNSV
410 420 430 440 450
GNLILSAEHQ GGNICIEVTD DGAGLNRERI LAKAASQGLT VSENMSDDEV
460 470 480 490 500
AMLIFAPGFS TAEQVTDVSG RGVGMDVVKR NIQKMGGHVE IQSKQGTGTT
510 520 530 540 550
IRILLPLTLA ILDGMSVRVA DEVFILPLNA VMESLQPREA DLHPLAGGER
560 570 580 590 600
VLEVRGEYLP IVELWKVFNV AGAKTEATQG IVVILQSGGR RYALLVDQLI
610 620 630 640 650
GQHQVVVKNL ESNYRKVPGI SAATILGDGS VALIVDVSAL QAINREQRMA

NTAA
Length:654
Mass (Da):71,382
Last modified:November 1, 1997 - v3
Checksum:i009B824154E269B4
GO
Isoform cheA(S) (identifier: P07363-2) [UniParc]FASTAAdd to basket

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661R → P in AAA23573 (PubMed:2002011).Curated
Sequence conflicti166 – 1661R → P in AAA23574 (PubMed:2002011).Curated
Sequence conflicti548 – 56518GERVL…IVELW → ASGCWKCGVNICPSSNCG in AAA23564 (PubMed:3510184).CuratedAdd
BLAST
Sequence conflicti606 – 6061V → A in AAA23564 (PubMed:3510184).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9797Missing in isoform cheA(S). CuratedVSP_018886Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PIRiH64951. QRECCS.
RefSeqiNP_416402.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74958; AAC74958; b1888.
BAA15709; BAA15709; BAA15709.
GeneIDi946401.
KEGGiecj:Y75_p1864.
eco:b1888.
PATRICi32119103. VBIEscCol129921_1969.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PIRiH64951. QRECCS.
RefSeqiNP_416402.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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-A124-262[»]
2LP4NMR-A1-225[»]
DisProtiDP00407.
ProteinModelPortaliP07363.
SMRiP07363. Positions 1-226, 261-640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP07363.
PRIDEiP07363.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74958; AAC74958; b1888.
BAA15709; BAA15709; BAA15709.
GeneIDi946401.
KEGGiecj:Y75_p1864.
eco:b1888.
PATRICi32119103. VBIEscCol129921_1969.

Organism-specific databases

EchoBASEiEB0144.
EcoGeneiEG10146. cheA.

Phylogenomic databases

eggNOGiCOG0643.
HOGENOMiHOG000255263.
InParanoidiP07363.
KOiK03407.
OMAiVQTIRVN.
OrthoDBiEOG62RS8P.
PhylomeDBiP07363.

Enzyme and pathway databases

BioCyciEcoCyc:CHEA-SMALL.
EcoCyc:PROTEIN-CHEA.
ECOL316407:JW1877-MONOMER.
RETL1328306-WGS:GSTH-3589-MONOMER.
BRENDAi2.7.13.3. 2026.

Miscellaneous databases

EvolutionaryTraceiP07363.
PROiP07363.

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_C.
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.
SSF55052. SSF55052. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS50851. CHEW. 1 hit.
PS50109. HIS_KIN. 1 hit.
PS50894. HPT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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 AT HIS-48, 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 informationi

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: June 24, 2015
This is version 160 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.