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P07363

- CHEA_ECOLI

UniProt

P07363 - CHEA_ECOLI

Protein

Chemotaxis protein CheA

Gene

cheA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      Previous versions | rss
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    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 binding Source: UniProtKB-KW
    2. phosphorelay sensor kinase activity Source: InterPro
    3. protein binding Source: IntAct

    GO - Biological processi

    1. chemotaxis Source: EcoCyc
    2. establishment of localization in cell Source: EcoCyc
    3. negative regulation of protein modification process Source: CACAO
    4. phosphorelay signal transduction system Source: EcoliWiki
    5. phosphorylation Source: EcoliWiki
    6. positive regulation of protein dephosphorylation Source: EcoCyc
    7. protein autophosphorylation Source: EcoliWiki

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10146. cheA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoCyc
    2. cytosol Source: EcoCyc
    3. plasma membrane Source: EcoCyc

    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 autocatalysis1 PublicationPROSITE-ProRule annotation

    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

    1
    654
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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-A124-262[»]
    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.
    KOiK03407.
    OMAiKISTPPM.
    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_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.
    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. Align

    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

    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]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:
    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.
    PIRiH64951. QRECCS.
    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 H64951. QRECCS.
    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 124-262 [» ]
    2LP4 NMR - A 1-225 [» ]
    DisProti DP00407.
    ProteinModelPortali P07363.
    SMRi P07363. Positions 1-226, 261-640.
    ModBasei Search...
    MobiDBi 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.
    PhylomeDBi P07363.

    Enzyme and pathway databases

    BioCyci EcoCyc:CHEA-SMALL.
    EcoCyc:PROTEIN-CHEA.
    ECOL316407:JW1877-MONOMER.
    RETL1328306-WGS:GSTH-3589-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.
    SSF55052. SSF55052. 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

    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: October 1, 2014
    This is version 155 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