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   25-MAY-2022, entry version 122.
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; Firmicutes; Bacilli; Bacillales; Listeriaceae; 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.lin0700; -.
DR   EnsemblBacteria; CAC95932; CAC95932; CAC95932.
DR   KEGG; lin:cheA; -.
DR   eggNOG; COG0643; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   HOGENOM; CLU_000650_3_6_9; -.
DR   OMA; MMDMAKS; -.
DR   OrthoDB; 305000at2; -.
DR   BRENDA; 2.7.13.3; 3044.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 1.10.287.560; -; 1.
DR   Gene3D; 1.20.120.160; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.30.70.1110; -; 1.
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; 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; 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; 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   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