(data stored in ACNUC7421 zone)

SWISSPROT: DCTS_BACSU

ID   DCTS_BACSU              Reviewed;         535 AA.
AC   P96601;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 146.
DE   RecName: Full=Probable C4-dicarboxylate sensor kinase;
DE            EC=2.7.13.3;
GN   Name=dctS; Synonyms=ydbF; OrderedLocusNames=BSU04450;
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;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION, AND GENE NAME.
RC   STRAIN=168;
RX   PubMed=10708364; DOI=10.1099/00221287-146-2-263;
RA   Asai K., Baik S.-H., Kasahara Y., Moriya S., Ogasawara N.;
RT   "Regulation of the transport system for C4-dicarboxylic acids in Bacillus
RT   subtilis.";
RL   Microbiology 146:263-271(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 DctS/DctR.
CC       Probably activates DctR by phosphorylation (By similarity). Essential
CC       for expression of dctP. {ECO:0000250, ECO:0000269|PubMed:10708364,
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}.
DR   EMBL; AB001488; BAA19282.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12252.1; -; Genomic_DNA.
DR   PIR; A69771; A69771.
DR   RefSeq; NP_388326.1; NC_000964.3.
DR   RefSeq; WP_003234348.1; NZ_JNCM01000031.1.
DR   SMR; P96601; -.
DR   STRING; 224308.BSU04450; -.
DR   PaxDb; P96601; -.
DR   PRIDE; P96601; -.
DR   DNASU; 938231; -.
DR   EnsemblBacteria; CAB12252; CAB12252; BSU04450.
DR   GeneID; 938231; -.
DR   KEGG; bsu:BSU04450; -.
DR   PATRIC; fig|224308.179.peg.471; -.
DR   eggNOG; ENOG4105CEQ; Bacteria.
DR   eggNOG; COG3290; LUCA.
DR   HOGENOM; HOG000241936; -.
DR   InParanoid; P96601; -.
DR   KO; K11691; -.
DR   OMA; NHEHMNK; -.
DR   PhylomeDB; P96601; -.
DR   BioCyc; BSUB:BSU04450-MONOMER; -.
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   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; 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; 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;
DR   PRODOM; P96601.
DR   SWISS-2DPAGE; P96601.
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..535
FT                   /note="Probable C4-dicarboxylate sensor kinase"
FT                   /id="PRO_0000074728"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..172
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..535
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          213..276
FT                   /note="PAS"
FT   DOMAIN          333..528
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         336
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   535 AA;  59942 MW;  614BDA8BE8F10CFE CRC64;
     MNKKKLSIRW KITILSYILV IFSFLIGGIV LIGNIQHTEE RELKKRLMNT ARTVSEMTEV
     KEALARKKQT EAVRHAVEEI RMINEADYIV VMDMNHIRYT HPVSTSIGKK SEGADEEAAF
     AEHIYFSEAK GEIGTAVRAF YPVKDQDLNQ IGVVLVGKTL PGIADILLHL KRDIAFIVVL
     TLGFGLAGSF LLARHIKKQM FQLEPHEIVR MYEERTATFH SMNEGVIAID NRLVITIFNE
     KAKQIFEVQG DLIGKVIWEV LKDSRLPEIV ERNKAVYNEE IRVSGKVIMS SRIPIVMKKK
     VIGAVAIFQD RTEAAKMAEE LTGVRNFVEA LRVQNHEHMN KLHTIAGLIQ LGKSEKALQL
     AFQASTEQEN VTEFLHRSIQ NDAAAGLLLS KIRRGRELGI AVHIDENSSL QQFPEHVDQH
     DIVVLLGNLI ENAFGSFETV QSEDKRIDIS IEQTDDILAI LIEDNGCGIE PTHMPRLYDK
     GFTVNKTGGT GYGLYLVKQI IDKGSGTIEV DSHAGQGTSF SIVFPMKGEE AQHGS
//

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