ID   CHEA_HALS3              Reviewed;         668 AA.
AC   B0R4J9; Q48297;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Chemotaxis protein CheA;
DE            EC=2.7.13.3;
GN   Name=cheA; OrderedLocusNames=OE_2415R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, FUNCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=R1 / S9;
RX   PubMed=7882970; DOI=10.1002/j.1460-2075.1995.tb07045.x;
RA   Rudolph J., Oesterhelt D.;
RT   "Chemotaxis and phototaxis require a CheA histidine kinase in the archaeon
RT   Halobacterium salinarium.";
RL   EMBO J. 14:667-673(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
RP   HIS-44.
RC   STRAIN=R1 / S9 / D2;
RX   PubMed=7556066; DOI=10.1002/j.1460-2075.1995.tb00099.x;
RA   Rudolph J., Tolliday N., Schmitt C., Schuster S.C., Oesterhelt D.;
RT   "Phosphorylation in halobacterial signal transduction.";
RL   EMBO J. 14:4249-4257(1995).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=8636990; DOI=10.1006/jmbi.1996.0267;
RA   Rudolph J., Oesterhelt D.;
RT   "Deletion analysis of the che operon in the archaeon Halobacterium
RT   salinarium.";
RL   J. Mol. Biol. 258:548-554(1996).
RN   [5]
RP   INTERACTION WITH CHEW1; CHEY AND TRANSDUCER PROTEINS.
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=23171228; DOI=10.1186/1471-2180-12-272;
RA   Schlesner M., Miller A., Besir H., Aivaliotis M., Streif J., Scheffer B.,
RA   Siedler F., Oesterhelt D.;
RT   "The protein interaction network of a taxis signal transduction system in a
RT   halophilic archaeon.";
RL   BMC Microbiol. 12:272-272(2012).
CC   -!- FUNCTION: Involved in the transmission of sensory signals from the
CC       chemoreceptors and photoreceptors to the flagellar motors.
CC       Autophosphorylates, probably in response to a chemo- or phototactic
CC       signal, and transfers its phosphate group to CheY. Could also transfer
CC       its phosphate group to CheB. {ECO:0000269|PubMed:7556066,
CC       ECO:0000269|PubMed:7882970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:7556066};
CC   -!- SUBUNIT: Interacts with CheW1, CheY, and several transducer proteins
CC       (HTR-I, HTR-II, BasT, CosT, MpcT, Htr4, Htr6, HtrVIII, Htr16 and
CC       Htr17). {ECO:0000269|PubMed:23171228}.
CC   -!- PTM: Autophosphorylated.
CC   -!- DISRUPTION PHENOTYPE: Deletion leads to the loss of both chemotactic
CC       and phototactic responses. {ECO:0000269|PubMed:7882970,
CC       ECO:0000269|PubMed:8636990}.
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; X82645; CAA57970.1; -; Genomic_DNA.
DR   EMBL; AM774415; CAP13664.1; -; Genomic_DNA.
DR   PIR; S54304; S54304.
DR   RefSeq; WP_010902690.1; NC_010364.1.
DR   AlphaFoldDB; B0R4J9; -.
DR   SMR; B0R4J9; -.
DR   EnsemblBacteria; CAP13664; CAP13664; OE_2415R.
DR   GeneID; 5953633; -.
DR   KEGG; hsl:OE_2415R; -.
DR   HOGENOM; CLU_000650_3_6_2; -.
DR   OMA; MMDMAKS; -.
DR   PhylomeDB; B0R4J9; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 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; 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   ATP-binding; Chemotaxis; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..668
FT                   /note="Chemotaxis protein CheA"
FT                   /id="PRO_0000429066"
FT   DOMAIN          1..101
FT                   /note="HPt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   DOMAIN          330..541
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          543..668
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT   REGION          123..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         44
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         44
FT                   /note="H->Q: Lack of phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:7556066"
FT   CONFLICT        128
FT                   /note="D -> H (in Ref. 1; CAA57970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="A -> V (in Ref. 1; CAA57970)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   668 AA;  71882 MW;  6C4D851F70F9BCB1 CRC64;
     MDDYLEAFVR EGEEHVTSLN NALLELESDP GNEEAMDEIF RTAHTLKGNF GAMGFEDASD
     LAHAVEDLLD EMRQGNLEVT SDRMDRIFEG IDGIEACLDE IQATGDVDRD VTGTIESVRA
     VLDEVDGDGG SGTTTSSGDA GSPAGDGDVD ATRVVDADTI DAAEDPVYHI HIDMGDSQMK
     GVDGMFVLEE ATEAFDLLGA EPSPDAINDG EYGDGFELVV ATPSDEVSDT VAAFPKLSDA
     TVTAVGDDEH APDADSGTEA DASADDDADD AGTTADSGSS SGGSSAIDNT DTEIQSVRVD
     VDQLDELHGL VEQLVTTRIK LRRGMEESDR EVLDELDELD KITSSLQDTV MDMRLVPMKK
     IVGKFPRLVR DLAREQDKDI DFVVEGDDVE LDRTILTEIS DPLMHLLRNA VDHGIEKPAV
     REDNGKDREG TITLSAERDR DHVLIQVRDD GAGIDHDTMR EKAIEKGVKT REEVQDMPDD
     DVEDLVFHPG FSTNDEVTDV SGRGVGMDVV RDTVTRLDGS VSVDSTPGEG TTFTMTLPVT
     VAIVKVLFVE SGGEEYGIPI KTVDEISRMK SVKSVDGEEV ITYDETVYPL VRLGDALNVP
     DETRNGDGML VRIRDSERQV AVHCDDVRGQ EEVVVKPFEG ILSGIPGLSG AAVLGEGDVV
     TILDVATL