ID   CITS_BACSU              Reviewed;         542 AA.
AC   O34427;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Sensor protein CitS;
DE            EC=2.7.13.3;
GN   Name=citS; Synonyms=yflR; OrderedLocusNames=BSU07580;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / AC327;
RX   PubMed=9272861; DOI=10.1016/s0378-1119(97)00130-3;
RA   Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT   "Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of
RT   the Bacillus subtilis genome reveal genes for a new two-component system,
RT   three spore germination proteins, an iron uptake system and a general
RT   stress response protein.";
RL   Gene 194:191-199(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   CHARACTERIZATION.
RC   STRAIN=168;
RX   PubMed=10972810; DOI=10.1046/j.1365-2958.2000.02055.x;
RA   Yamamoto H., Murata M., Sekiguchi J.;
RT   "The CitST two-component system regulates the expression of the Mg-citrate
RT   transporter in Bacillus subtilis.";
RL   Mol. Microbiol. 37:898-912(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=11717295; DOI=10.1128/jb.183.24.7365-7370.2001;
RA   Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T.,
RA   Fujita Y.;
RT   "Comprehensive DNA microarray analysis of Bacillus subtilis two-component
RT   regulatory systems.";
RL   J. Bacteriol. 183:7365-7370(2001).
CC   -!- FUNCTION: Member of the two-component regulatory system CitT/CitS.
CC       Regulates the expression of the citM-yflN operon. Functions probably as
CC       a membrane-associated protein kinase that phosphorylates CitT in
CC       response to environmental citrate or Mg(2+)-citrate complex.
CC       {ECO:0000269|PubMed:11717295}.
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; D86417; BAA22311.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12587.1; -; Genomic_DNA.
DR   PIR; E69600; E69600.
DR   RefSeq; NP_388639.1; NC_000964.3.
DR   RefSeq; WP_003242967.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; O34427; -.
DR   SMR; O34427; -.
DR   IntAct; O34427; 23.
DR   STRING; 224308.BSU07580; -.
DR   PaxDb; O34427; -.
DR   DNASU; 939687; -.
DR   EnsemblBacteria; CAB12587; CAB12587; BSU_07580.
DR   GeneID; 939687; -.
DR   KEGG; bsu:BSU07580; -.
DR   PATRIC; fig|224308.179.peg.823; -.
DR   eggNOG; COG3290; Bacteria.
DR   InParanoid; O34427; -.
DR   OMA; QNGFITM; -.
DR   PhylomeDB; O34427; -.
DR   BioCyc; BSUB:BSU07580-MON; -.
DR   BRENDA; 2.7.13.3; 658.
DR   Proteomes; UP000001570; 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; IBA:GO_Central.
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; IPR035965; PAS-like_dom_sf.
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; PF14689; SPOB_a; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 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   1: Evidence at protein level;
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..542
FT                   /note="Sensor protein CitS"
FT                   /id="PRO_0000074735"
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..175
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..542
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          216..279
FT                   /note="PAS"
FT   DOMAIN          336..528
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   542 AA;  59891 MW;  E0F3BBB9792F8C42 CRC64;
     MVKKRFHFSL QTKIMGLIAA LLVFVIGVLT ITLAVQHTQG ERRQAEQLAV QTARTISYMP
     PVKELIERKD GHAAQTQEVI EQMKEQTGAF AIYVLNEKGD IRSASGKSGL KKLERSREIL
     FGGSHVSETK ADGRRVIRGS APIIKEQKGY SQVIGSVSVD FLQTETEQSI KKHLRNLSVI
     AVLVLLLGFI GAAVLAKSIR KDTLGLEPHE IAALYRERNA MLFAIREGII ATNREGVVTM
     MNVSAAEMLK LPEPVIHLPI DDVMPGAGLM SVLEKGEMLP NQEVSVNDQV FIINTKVMNQ
     GGQAYGIVVS FREKTELKKL IDTLTEVRKY SEDLRAQTHE FSNKLYAILG LLELGEYDEA
     IDLIKEEYAI QNEQHDLLFH NIHSQQVQAI LLGKISKASE KKVKLVIDEN SSLAPLPAHI
     GLSHLITIIG NLIDNAFEAV AEQSVKEVLF FITDMGHDIV IEVSDTGPGV PPEKIEAVFE
     RGYSSKGMRR GYGLANVKDS VRELGGWIEL ANQKTGGAVF TVFIPKEKQR GNPFDSHRDC
     GG