ID   CHEA_CERSP              Reviewed;         686 AA.
AC   Q53135;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Chemotaxis protein CheA;
DE            EC=2.7.13.3;
GN   Name=cheA;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WS8N;
RX   PubMed=7494484; DOI=10.1111/j.1365-2958.1995.mmi_17020357.x;
RA   Ward M.J., Bell A.W., Hamblin P.A., Packer H.L., Armitage J.P.;
RT   "Identification of a chemotaxis operon with two cheY genes in Rhodobacter
RT   sphaeroides.";
RL   Mol. Microbiol. 17:357-366(1995).
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}.
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DR   EMBL; X80027; CAA56330.1; -; Genomic_DNA.
DR   PIR; S70180; S70180.
DR   RefSeq; WP_002719591.1; NZ_CP033450.1.
DR   AlphaFoldDB; Q53135; -.
DR   SMR; Q53135; -.
DR   PRIDE; Q53135; -.
DR   BRENDA; 2.7.13.3; 5383.
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   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; 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   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; 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..686
FT                   /note="Chemotaxis protein CheA"
FT                   /id="PRO_0000074717"
FT   DOMAIN          1..106
FT                   /note="HPt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   DOMAIN          290..540
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          542..678
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT   REGION          253..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   686 AA;  74291 MW;  167B6B8BDF756E03 CRC64;
     MDQSDIRSAF FVECEDLMEA LNEGLDRIED TLDDGHDDET VNAVFRAVHS IKGGAGAFKL
     DALVRFAHQF ETTLDALRAG RVSADPPLLA LLHKAADRLS DLLQAARTGS ETATIDPDDL
     VAQLAQAAGE EEAGEADAED LGFVPMRLDL DLPAAAPDEG QSGCYSIDFS PTRALYACGN
     DTSILFRVLS DLGRMEVRLD RSRLPDFDAL DWQESWLDWH LTLETDEPEH QIDEVFEFVE
     DLCRLEIRPM AMEAPRTDPD PEPDPEPDPP ASGPAAAKKS PAEDHRTSSP RATVRVELDR
     VDRLINIVGE LVINQAMLSQ CVQDEGVPPR SPVRNRLDDF RNLAREIQES VMAIRAQAIK
     PLFQRMSRIA REASEISQKQ IRLVTEGEST EVDKTVIERL ADPLTHMIRN AVDHGIEPAD
     RRLHLGKPPV GLITLTAAHR SGRVLIEIKD DGAGINRPRV LEIAQGKGLV AQDAQLTEEE
     IDGLLFMPGF STASVVSDLS GRGVGMDVVK SAIESLGGRI TIASDPGVGT TFTISLPLTL
     AVLDGMVVDV GGQTMVVPVS AIVETLRPRP ADIHVLGSGD QVVAIRGSLV PIVDCGSIFG
     FRAPVRSYEE SVLLLVETAR QKLCALVVDT IHDQRQVVIK GLENGYGRIP GVAAATILGD
     GRIALIIAPE EAVDIGTSGG TFSMEF