ID   DCTS_RHOCA              Reviewed;         657 AA.
AC   P37739;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=C4-dicarboxylate transport sensor protein DctS;
DE            EC=2.7.13.3;
GN   Name=dctS;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=8455557; DOI=10.1007/bf00282803;
RA   Hamblin M.J., Shaw J.G., Kelly D.J.;
RT   "Sequence analysis and interposon mutagenesis of a sensor-kinase (DctS) and
RT   response-regulator (DctR) controlling synthesis of the high-affinity C4-
RT   dicarboxylate transport system in Rhodobacter capsulatus.";
RL   Mol. Gen. Genet. 237:215-224(1993).
CC   -!- FUNCTION: Member of the two-component regulatory system DctS/DctR
CC       involved in the transport of C4-dicarboxylates. DctS functions as a
CC       membrane-associated protein kinase that phosphorylates DctR in response
CC       to environmental signals.
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 inner membrane; Multi-pass membrane protein.
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DR   EMBL; X64733; CAA45999.1; -; Genomic_DNA.
DR   PIR; S30288; S30288.
DR   AlphaFoldDB; P37739; -.
DR   SMR; P37739; -.
DR   BRENDA; 2.7.13.3; 5381.
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; cd00082; HisKA; 1.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..657
FT                   /note="C4-dicarboxylate transport sensor protein DctS"
FT                   /id="PRO_0000074749"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..252
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        274..657
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          289..361
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          365..417
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          437..652
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          407..422
FT                   /note="Inter-domain linker"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         440
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   657 AA;  70143 MW;  139D2CFC7CFFA69B CRC64;
     MRDTTGGPAG AEVWTVPGLL GARKLDLLAL IPLVAIVALM TLVGALLFAV AQSDANRARA
     KLATDALWVE QTLRFQMAVD EDVLVRLALD ASAGASQQAL SARARLHLAA NPETLGLRWY
     DATGRLIAAV PEGPGPAEAA LVRQLLASGA LPPRPVYGPV RDGRVVLAER VSASGGVVVA
     TVSLPMMLER HLPWWIAEQY GVRISDTSGV LAERARRPIA AAAPRHGISF DPPLAGTTLE
     IMAYDAPDAF GNAALLAAIG ALSVFAVLAM VVLHRNALRR RMAEDRLRAE MAFRRAMEES
     LTVGMRAKDL SGRILYVNGA FCKLVGLAAE DLVGRAQPMP YWAPDFLEET LARQRQLIEG
     QPVPQAFETR FRRSDGSEIE VQVFEAPLID AGGRHRGWMG SVIDITQAKQ AARLARAQDE
     SLARTGRLVT LGEMASTLAH ELNQPLAAIA SYAAGGLNLF DQPEPNLTML RQAFEKMGAQ
     ARRAGLVIRR VQDFVKKRTP QLAALDLSEV LAEALSITAP VAREHRVKLA SLIEGRIPGV
     QADRILIEQV LVNLIRNGVE AMAEGPRTGD DLTVRLARAG AAVTIEVMDR GPGISDAVAA
     SLFDPFTSTK SEGMGMGLNI CRSIVEMHHG SLSHGPRAGG GTVFTVTLPV PQEGAPA