CHEA_ECOLI
ID CHEA_ECOLI Reviewed; 654 AA.
AC P07363; P76302;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 25-MAY-2022, entry version 200.
DE RecName: Full=Chemotaxis protein CheA;
DE EC=2.7.13.3;
GN Name=cheA; OrderedLocusNames=b1888, JW1877;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2002011; DOI=10.1128/jb.173.6.2116-2119.1991;
RA Kofoid E.C., Parkinson J.S.;
RT "Tandem translation starts in the cheA locus of Escherichia coli.";
RL J. Bacteriol. 173:2116-2119(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-654.
RX PubMed=3510184; DOI=10.1128/jb.165.1.161-166.1986;
RA Mutoh N., Simon M.I.;
RT "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia
RT coli.";
RL J. Bacteriol. 165:161-166(1986).
RN [6]
RP PHOSPHORYLATION AT HIS-48, AND DOMAINS.
RX PubMed=2832069; DOI=10.1016/0092-8674(88)90490-4;
RA Oosawa K., Hess J.F., Simon M.I.;
RT "Mutants defective in bacterial chemotaxis show modified protein
RT phosphorylation.";
RL Cell 53:89-96(1988).
RN [7]
RP SUBUNIT.
RX PubMed=2068106; DOI=10.1073/pnas.88.14.6269;
RA McNally D.F., Matsumura P.;
RT "Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex
RT enhances autophosphorylation and affinity for CheY.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6269-6273(1991).
RN [8]
RP STRUCTURE BY NMR OF 1-233.
RX PubMed=8555213; DOI=10.1021/bi951960e;
RA Zhou H., McEvoy M.M., Lowry D.F., Swanson R.V., Simon M.I., Dahlquist F.W.;
RT "Phosphotransfer and CheY-binding domains of the histidine autokinase CheA
RT are joined by a flexible linker.";
RL Biochemistry 35:433-443(1996).
RN [9]
RP STRUCTURE BY NMR OF 124-257.
RX PubMed=8639521; DOI=10.1021/bi952707h;
RA McEvoy M.M., Muhandiram D.R., Kyw L.E., Dahlquist F.W.;
RT "Structure and dynamics of a CheY-binding domain of the chemotaxis kinase
RT CheA determined by nuclear magnetic resonance spectroscopy.";
RL Biochemistry 35:5633-5640(1996).
RN [10]
RP STRUCTURE BY NMR OF 1-134.
RX PubMed=9020767; DOI=10.1021/bi961663p;
RA Zhou H., Dahlquist F.W.;
RT "Phosphotransfer site of the chemotaxis-specific protein kinase CheA as
RT revealed by NMR.";
RL Biochemistry 36:699-710(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 158-228.
RX PubMed=9437425; DOI=10.1038/nsb0198-25;
RA Welch M., Chinardet N., Mourey L., Birck C., Samama J.-P.;
RT "Structure of the CheY-binding domain of histidine kinase CheA in complex
RT with CheY.";
RL Nat. Struct. Biol. 5:25-29(1998).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 158-226.
RX PubMed=9636149; DOI=10.1073/pnas.95.13.7333;
RA McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., Dahlquist F.W.;
RT "Two binding modes reveal flexibility in kinase/response regulator
RT interactions in the bacterial chemotaxis pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7333-7338(1998).
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: An in vitro complex of CheW/CheA(L)/CheA(S) in a 1:1:1 ratio
CC increases the autophosphorylation of CheA and is required for the
CC binding of CheY, the phosphorylation substrate. This complex accounts
CC for 10% of the total number of molecules. {ECO:0000269|PubMed:2068106}.
CC -!- INTERACTION:
CC P07363; P07330: cheB; NbExp=3; IntAct=EBI-1026773, EBI-1125895;
CC P07363; P0AE67: cheY; NbExp=7; IntAct=EBI-1026773, EBI-546693;
CC P07363; P0A9H9: cheZ; NbExp=3; IntAct=EBI-1026773, EBI-546726;
CC P07363; P07017: tar; NbExp=4; IntAct=EBI-1026773, EBI-1125130;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=cheA(L); Synonyms=long, large;
CC IsoId=P07363-1; Sequence=Displayed;
CC Name=cheA(S); Synonyms=short;
CC IsoId=P07363-2; Sequence=VSP_018886;
CC -!- DOMAIN: May have three functional domains: one for interaction with
CC CheB and CheY, a second for regulating phosphorylation and controlling
CC the stability of the protein, and a third for receiving input signals
CC regulating CheA activity. {ECO:0000269|PubMed:2832069}.
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DR EMBL; M34669; AAA23573.1; -; Genomic_DNA.
DR EMBL; M34669; AAA23574.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74958.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15709.1; -; Genomic_DNA.
DR EMBL; M13462; AAA23564.1; -; Genomic_DNA.
DR PIR; H64951; QRECCS.
DR RefSeq; NP_416402.1; NC_000913.3.
DR RefSeq; WP_001350517.1; NZ_LN832404.1.
DR PDB; 1A0O; X-ray; 2.95 A; B/D/F/H=124-257.
DR PDB; 1EAY; X-ray; 2.00 A; C/D=156-228.
DR PDB; 1FFG; X-ray; 2.10 A; B/D=124-257.
DR PDB; 1FFS; X-ray; 2.40 A; B/D=124-257.
DR PDB; 1FFW; X-ray; 2.70 A; B/D=124-257.
DR PDB; 1FWP; NMR; -; A=124-262.
DR PDB; 2LP4; NMR; -; A=1-225.
DR PDB; 6S1K; EM; 8.38 A; A/B=1-654.
DR PDBsum; 1A0O; -.
DR PDBsum; 1EAY; -.
DR PDBsum; 1FFG; -.
DR PDBsum; 1FFS; -.
DR PDBsum; 1FFW; -.
DR PDBsum; 1FWP; -.
DR PDBsum; 2LP4; -.
DR PDBsum; 6S1K; -.
DR AlphaFoldDB; P07363; -.
DR SMR; P07363; -.
DR BioGRID; 4261034; 200.
DR ComplexPortal; CPX-1077; Chemotaxis phosphorelay complex CheA-CheY.
DR DIP; DIP-6053N; -.
DR IntAct; P07363; 33.
DR STRING; 511145.b1888; -.
DR BindingDB; P07363; -.
DR ChEMBL; CHEMBL4295999; -.
DR iPTMnet; P07363; -.
DR PaxDb; P07363; -.
DR PRIDE; P07363; -.
DR EnsemblBacteria; AAC74958; AAC74958; b1888.
DR EnsemblBacteria; BAA15709; BAA15709; BAA15709.
DR GeneID; 946401; -.
DR KEGG; ecj:JW1877; -.
DR KEGG; eco:b1888; -.
DR PATRIC; fig|511145.12.peg.1969; -.
DR EchoBASE; EB0144; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_6; -.
DR InParanoid; P07363; -.
DR OMA; MMDMAKS; -.
DR PhylomeDB; P07363; -.
DR BRENDA; 2.7.13.3; 2026.
DR EvolutionaryTrace; P07363; -.
DR PHI-base; PHI:6535; -.
DR PRO; PR:P07363; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0098561; C:methyl accepting chemotaxis protein complex; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:CACAO.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:CAFA.
DR GO; GO:0009454; P:aerotaxis; IDA:EcoCyc.
DR GO; GO:0071977; P:bacterial-type flagellum-dependent swimming motility; IDA:ComplexPortal.
DR GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:EcoCyc.
DR GO; GO:0031400; P:negative regulation of protein modification process; IDA:CACAO.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IMP:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoliWiki.
DR GO; GO:0016310; P:phosphorylation; IDA:EcoliWiki.
DR GO; GO:1901875; P:positive regulation of post-translational protein modification; IDA:CAFA.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoliWiki.
DR GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IDA:CAFA.
DR GO; GO:0050920; P:regulation of chemotaxis; IDA:CAFA.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR GO; GO:0043052; P:thermotaxis; IDA:EcoCyc.
DR CDD; cd00088; HPT; 1.
DR DisProt; DP00407; -.
DR Gene3D; 1.10.287.560; -; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.30.70.400; -; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR015162; CheY-binding.
DR InterPro; IPR035891; CheY-binding_CheA.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF09078; CheY-binding; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF50341; SSF50341; 1.
DR SUPFAM; SSF55052; SSF55052; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; ATP-binding; Chemotaxis; Cytoplasm;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Two-component regulatory system.
FT CHAIN 1..654
FT /note="Chemotaxis protein CheA"
FT /id="PRO_0000032373"
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT DOMAIN 257..509
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 511..646
FT /note="CheW-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT MOD_RES 48
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:2832069"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform cheA(S))"
FT /evidence="ECO:0000305"
FT /id="VSP_018886"
FT CONFLICT 166
FT /note="R -> P (in Ref. 1; AAA23573/AAA23574)"
FT /evidence="ECO:0000305"
FT CONFLICT 548..565
FT /note="GERVLEVRGEYLPIVELW -> ASGCWKCGVNICPSSNCG (in Ref. 5;
FT AAA23564)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="V -> A (in Ref. 5; AAA23564)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:2LP4"
FT HELIX 9..29
FT /evidence="ECO:0007829|PDB:2LP4"
FT HELIX 37..56
FT /evidence="ECO:0007829|PDB:2LP4"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:2LP4"
FT HELIX 85..106
FT /evidence="ECO:0007829|PDB:2LP4"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:2LP4"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2LP4"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2LP4"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1EAY"
FT HELIX 171..182
FT /evidence="ECO:0007829|PDB:1EAY"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1EAY"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1EAY"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1FWP"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:1EAY"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1EAY"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1EAY"
SQ SEQUENCE 654 AA; 71382 MW; 009B824154E269B4 CRC64;
MSMDISDFYQ TFFDEADELL ADMEQHLLVL QPEAPDAEQL NAIFRAAHSI KGGAGTFGFS
VLQETTHLME NLLDEARRGE MQLNTDIINL FLETKDIMQE QLDAYKQSQE PDAASFDYIC
QALRQLALEA KGETPSAVTR LSVVAKSEPQ DEQSRSQSPR RIILSRLKAG EVDLLEEELG
HLTTLTDVVK GADSLSAILP GDIAEDDITA VLCFVIEADQ ITFETVEVSP KISTPPVLKL
AAEQAPTGRV EREKTTRSNE STSIRVAVEK VDQLINLVGE LVITQSMLAQ RSSELDPVNH
GDLITSMGQL QRNARDLQES VMSIRMMPME YVFSRYPRLV RDLAGKLGKQ VELTLVGSST
ELDKSLIERI IDPLTHLVRN SLDHGIELPE KRLAAGKNSV GNLILSAEHQ GGNICIEVTD
DGAGLNRERI LAKAASQGLT VSENMSDDEV AMLIFAPGFS TAEQVTDVSG RGVGMDVVKR
NIQKMGGHVE IQSKQGTGTT IRILLPLTLA ILDGMSVRVA DEVFILPLNA VMESLQPREA
DLHPLAGGER VLEVRGEYLP IVELWKVFNV AGAKTEATQG IVVILQSGGR RYALLVDQLI
GQHQVVVKNL ESNYRKVPGI SAATILGDGS VALIVDVSAL QAINREQRMA NTAA
