ID   CITS_ALKHC              Reviewed;         538 AA.
AC   Q9RC53;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Sensor protein CitS;
DE            EC=2.7.13.3;
GN   Name=citS; OrderedLocusNames=BH3839;
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 [GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=10484179; DOI=10.1007/s007920050120;
RA   Takami H., Takaki Y., Nakasone K., Sakiyama T., Maeno G., Sasaki R.,
RA   Hirama C., Fuji F., Masui N.;
RT   "Genetic analysis of the chromosome of alkaliphilic Bacillus halodurans C-
RT   125.";
RL   Extremophiles 3:227-233(1999).
RN   [2]
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 CitT/CitS.
CC       Functions probably as a membrane-associated protein kinase that
CC       phosphorylates CitT in response to environmental citrate or Mg(2+)-
CC       citrate complex (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; AB024561; BAA83946.1; -; Genomic_DNA.
DR   EMBL; BA000004; BAB07558.1; -; Genomic_DNA.
DR   PIR; G84129; G84129.
DR   RefSeq; WP_010899964.1; NC_002570.2.
DR   AlphaFoldDB; Q9RC53; -.
DR   STRING; 272558.10176464; -.
DR   EnsemblBacteria; BAB07558; BAB07558; BAB07558.
DR   KEGG; bha:BH3839; -.
DR   eggNOG; COG3290; Bacteria.
DR   HOGENOM; CLU_020211_11_2_9; -.
DR   OMA; HIESNYV; -.
DR   OrthoDB; 1755994at2; -.
DR   BRENDA; 2.7.13.3; 661.
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..538
FT                   /note="Sensor protein CitS"
FT                   /id="PRO_0000074734"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..174
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..538
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          216..282
FT                   /note="PAS"
FT   DOMAIN          339..534
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         342
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   538 AA;  59814 MW;  A679B7A0D7662668 CRC64;
     MKRRLFPLTF SAKMMGFIAL LIIAMFVLLG VFLNEQYART LEEQMGERAL SVAQAVALIP
     ELREAFSAER PDEIIQPIAE SIRVETGAEF IVVGNTDLIR YAHPLPERIG QRMVGGDNER
     ALVHGESYVS KAVGSLGPSI RGKVPVFDDN GKIIGIVSVG FLMEDIQQVI GERLIAMWQI
     VVVIMILGLM GTWLVANTVK KATLGLEPEE IGQQFQQKEA ILQSIHEGVI AVNKEGKVTL
     FNQAAMKYVD PELDKEDVLG RHVTDLVKHT RLPEVLQVGK GQYDQELRIG DKQAVVNRVP
     IYYDHEIVGA VATFRDRNEI KKLSEELTNV KNYADALRAQ THEFSNKLNT ISGFLQLGKI
     DEAVDFIQKE RKIQQEWIHF FIERVNDPTV SAVLLGKISQ AQELGIDVDI DPSSQLLTPL
     QERQQELLVT MIGNLLENAF DALLASGIEN KKIYISFTDM GDDFIFEVED NGPGIPPQLM
     ESIFEEGFST KEGTHRGFGL ALVKKAVHEL GGAIFLEEGE LGGACFVLTI PKHEAKEG