ID   DCTS_ALKHC              Reviewed;         532 AA.
AC   Q9K997;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Probable C4-dicarboxylate sensor kinase;
DE            EC=2.7.13.3;
GN   Name=dctS; OrderedLocusNames=BH2752;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Member of the two-component regulatory system DctS/DctR.
CC       Probably activates DctR by phosphorylation. Essential for expression of
CC       dctP (By 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: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; BA000004; BAB06471.1; -; Genomic_DNA.
DR   PIR; H83993; H83993.
DR   RefSeq; WP_010898900.1; NC_002570.2.
DR   AlphaFoldDB; Q9K997; -.
DR   SMR; Q9K997; -.
DR   STRING; 272558.10175373; -.
DR   DNASU; 893487; -.
DR   EnsemblBacteria; BAB06471; BAB06471; BAB06471.
DR   KEGG; bha:BH2752; -.
DR   eggNOG; COG3290; Bacteria.
DR   HOGENOM; CLU_020211_11_2_9; -.
DR   OMA; NHEHMNK; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF103190; SSF103190; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF55890; SSF55890; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..532
FT                   /note="Probable C4-dicarboxylate sensor kinase"
FT                   /id="PRO_0000074727"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..175
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..532
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          216..279
FT                   /note="PAS"
FT   DOMAIN          315..531
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         339
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   532 AA;  59999 MW;  5C2445CEA0119A12 CRC64;
     MRLFRQLSIQ WKITILSFGI VAFALMMVSI SLLGYVTSIK EDELSNRTMI TAQLVAQNHT
     VQQWVDAKPE EASRTLQPIV ERIRVINDHD YIVLLNMDRI RITHPIPERL QTPFVGGDED
     PAFAEHIYLS KAKTEGVVTV RAFMPILNQQ REQVGVAVVG SVLPSYADMI QEFWQPALLI
     GLITALFGFW GSWLLASHIK RQTFNMEPDE LAHLLVERDA SFNAIHEGVV AINKHEKITI
     MNEAARRMLG VKEKAIGRNI HEVIPDTKLP EILSIGKPLY QREFYIQGRL VFSNRIPIQI
     DGETVGAIAI FQDKSDVDRL AEELTGVQAF VDALRVQNHE YSNKLHTIAG LIQLDEGKKA
     LQYIFDLEEE QEEFSGVVMQ KIHNDSLAGL LLGKVSRGKE LGVQVIIEKD SEFIDHPEGV
     TTHDLVVIVG NLIDNSLDAF SSTQDQNKTV HVFIGEENDF LKIRVRDNGE GIREEVREKM
     FVRGFSTKST SGRGIGLFLI QAIVERVEGK IEVESELNIG TTFSIYLPKK RG