ID CHEA_LISIN Reviewed; 618 AA. AC Q92DW2; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 02-SEP-2026, entry version 134. DE RecName: Full=Chemotaxis protein CheA; DE EC=2.7.13.3; GN Name=cheA; OrderedLocusNames=lin0700; OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Listeriaceae; OC Listeria. OX NCBI_TaxID=272626; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-680 / CLIP 11262; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D., RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). 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 (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- CC histidine.; EC=2.7.13.3; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. 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; AL596166; CAC95932.1; -; Genomic_DNA. DR PIR; AD1520; AD1520. DR RefSeq; WP_010990559.1; NC_003212.1. DR AlphaFoldDB; Q92DW2; -. DR SMR; Q92DW2; -. DR STRING; 272626.gene:17565027; -. DR KEGG; lin:cheA; -. DR eggNOG; COG0643; Bacteria. DR eggNOG; COG2198; Bacteria. DR HOGENOM; CLU_000650_3_6_9; -. DR OrthoDB; 9803176at2; -. DR BRENDA; 2.7.13.3; 3044. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:InterPro. DR CDD; cd00731; CheA_reg; 1. DR CDD; cd16916; HATPase_CheA-like; 1. DR CDD; cd00088; HPT; 1. DR FunFam; 3.30.565.10:FF:000016; Chemotaxis protein CheA, putative; 1. DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1. DR Gene3D; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding 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; IPR051315; Bact_Chemotaxis_CheA. DR InterPro; IPR004105; CheA-like_dim. DR InterPro; IPR037006; CheA-like_homodim_sf. DR InterPro; IPR037052; CheA-like_P2_sf. DR InterPro; IPR010808; CheA_P2-bd. DR InterPro; IPR036061; CheW-like_dom_sf. DR InterPro; IPR002545; CheW-lke_dom. DR InterPro; IPR035891; CheY-binding_CheA. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. 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:SF1; CHEMOTAXIS PROTEIN CHEA; 1. DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1. DR Pfam; PF01584; CheW; 1. DR Pfam; PF02895; H-kinase_dim; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01627; Hpt; 1. DR Pfam; PF07194; P2; 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 3: Inferred from homology; KW ATP-binding; Chemotaxis; Cytoplasm; Kinase; Nucleotide-binding; KW Phosphoprotein; Transferase; Two-component regulatory system. FT CHAIN 1..618 FT /note="Chemotaxis protein CheA" FT /id="PRO_0000074714" FT DOMAIN 1..102 FT /note="HPt" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110" FT DOMAIN 233..488 FT /note="Histidine kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" FT DOMAIN 490..618 FT /note="CheW-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052" FT MOD_RES 45 FT /note="Phosphohistidine; by autocatalysis" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107" SQ SEQUENCE 618 AA; 68669 MW; 4302DAA45BDAB458 CRC64; MTTNMLDLFI EEASEHLQAL NDNLLQLEKD PTNGQLVSEI FRSAHTFKGM SATMGFQQVA DLTHAMENVL DEVRNNRLAV TEHLVDIIFT CTSHLETMVS DIQHGGQGAA DISKTVADLE ALLHPEQETD TAVEKTYRIA IQIEEAAILK AVRAVMCLER LAEMGIISET TPDREAIELE EFEHSFEVVL ETAQTKEEIE AVILDISEIE KVTVTEEVEE VQIIEPIKKA AKQTTKRLEN KTIRVQLEKI EKLMNVFEES VIERARIDEI AEKTNNKELM EHLGRFSSIS KEIQNGLLNM RMVPVDSVFN RFPKMVRTLA KELGKKIDLV IEGADTEVDK IVIDEIGDPL VHLIRNSVDH GAETVEVRRK NGKNETATIN LKAFHSGNNV VIEIVDDGAG INKRKVLEKA IAKNVVTRAE STKMTDSEIF DLLFDSGFST ADQVSDLSGR GVGLDVVRNT ILKIGGKISV ESSENAGSTF RIEIPLTLSI IQSMLVATSE RRYAVPLANV AEAITINPAD IQHVHGKDLI NYRETIIEVL DLGECFHETP LTDTDELLLL VVKNAKRTFG LIIKDIIGQR EIVLKTLGGF FSESQIAFSG ATILGDGRVV LILNLETF //