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 27-MAR-2024, entry version 206. DE RecName: Full=Chemotaxis protein CheA; DE EC=2.7.13.3; GN Name=cheA; GN OrderedLocusNames=b1888 {ECO:0000312|EMBL:AAC74958.2}, JW1877; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M34669; AAA23573.1; -; Genomic_DNA. DR EMBL; M34669; AAA23574.1; -; Genomic_DNA. DR EMBL; U00096; AAC74958.2; -; Genomic_DNA. DR EMBL; U00096; UMR55122.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15709.1; -; Genomic_DNA. DR EMBL; AH000879; 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 PDB; 8C5V; EM; 12.00 A; A/B=257-647, C/D=1-131. 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 PDBsum; 8C5V; -. DR AlphaFoldDB; P07363; -. DR EMDB; EMD-15641; -. DR EMDB; EMD-3234; -. DR EMDB; EMD-6319; -. DR EMDB; EMD-6320; -. 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; 511145-b1888; -. DR EnsemblBacteria; AAC74958; AAC74958; b1888. 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; HSGNHVF; -. DR OrthoDB; 9803176at2; -. 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: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: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; cd00731; CheA_reg; 1. DR CDD; cd16916; HATPase_CheA-like; 1. DR CDD; cd00088; HPT; 1. DR DisProt; DP00407; -. DR Gene3D; 3.30.70.400; CheY-binding domain of CheA; 1. DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 1.20.120.160; HPT domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1. DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1. 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF50341; CheW-like; 1. DR SUPFAM; SSF55052; CheY-binding domain of CheA; 1. DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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 //