ID CITS_HALH5 Reviewed; 538 AA. AC Q9RC53; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 02-SEP-2026, entry version 144. DE RecName: Full=Sensor protein CitS; DE EC=2.7.13.3; GN Name=citS; OrderedLocusNames=BH3839; OS Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 OS / JCM 9153 / C-125) (Bacillus halodurans). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Halalkalibacterium (ex Joshi et al. 2022). 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}. 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; 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 SMR; Q9RC53; -. DR STRING; 272558.gene:10729752; -. DR KEGG; bha:BH3839; -. DR eggNOG; COG3290; Bacteria. DR HOGENOM; CLU_020211_11_2_9; -. DR OrthoDB; 9792686at2; -. DR BRENDA; 2.7.13.3; 661. DR Proteomes; UP000001258; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR CDD; cd16915; HATPase_DpiB-CitA-like; 1. DR CDD; cd00130; PAS; 1. DR CDD; cd18773; PDC1_HK_sensor; 1. DR FunFam; 3.30.450.20:FF:000018; Sensor histidine kinase DcuS; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 2. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. 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 PANTHER; PTHR43547:SF3; SENSOR PROTEIN CITS; 1. DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1. 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1. DR SUPFAM; SSF103190; Sensory domain-like; 1. DR SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 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 //