ID   DCUS_ECOLI              Reviewed;         543 AA.
AC   P0AEC8; P39272; P76795; Q2M6H9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   02-SEP-2026, entry version 160.
DE   RecName: Full=Sensor histidine kinase DcuS {ECO:0000305};
DE            EC=2.7.13.3 {ECO:0000305|PubMed:12167640};
DE   AltName: Full=Fumarate sensor;
GN   Name=dcuS {ECO:0000303|PubMed:9765574, ECO:0000303|PubMed:9973351};
GN   Synonyms=yjdH; OrderedLocusNames=b4125, JW4086;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=9765574; DOI=10.1128/jb.180.20.5421-5425.1998;
RA   Zientz E., Bongaerts J., Unden G.;
RT   "Fumarate regulation of gene expression in Escherichia coli by the DcuSR
RT   (dcuSR genes) two-component regulatory system.";
RL   J. Bacteriol. 180:5421-5425(1998).
RN   [5]
RP   FUNCTION, AND TOPOLOGY.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=9973351; DOI=10.1128/jb.181.4.1238-1248.1999;
RA   Golby P., Davies S., Kelly D.J., Guest J.R., Andrews S.C.;
RT   "Identification and characterization of a two-component sensor-kinase and
RT   response-regulator system (DcuS-DcuR) controlling gene expression in
RT   response to C4-dicarboxylates in Escherichia coli.";
RL   J. Bacteriol. 181:1238-1248(1999).
RN   [6]
RP   FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND
RP   AUTOPHOSPHORYLATION.
RC   STRAIN=K12 / AN387;
RX   PubMed=12167640; DOI=10.1074/jbc.m204482200;
RA   Janausch I.G., Garcia-Moreno I., Unden G.;
RT   "Function of DcuS from Escherichia coli as a fumarate-stimulated histidine
RT   protein kinase in vitro.";
RL   J. Biol. Chem. 277:39809-39814(2002).
RN   [7]
RP   TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [8]
RP   ACTIVITY REGULATION, AND INTERACTION WITH DCTA AND DCUB.
RX   PubMed=27318186; DOI=10.1111/1462-2920.13418;
RA   Woerner S., Strecker A., Monzel C., Zeltner M., Witan J., Ebert-Jung A.,
RA   Unden G.;
RT   "Conversion of the sensor kinase DcuS of Escherichia coli of the DcuB/DcuS
RT   sensor complex to the C4-dicarboxylate responsive form by the transporter
RT   DcuB.";
RL   Environ. Microbiol. 18:4920-4930(2016).
RN   [9] {ECO:0007744|PDB:1OJG}
RP   STRUCTURE BY NMR OF 45-180, DOMAIN PERIPLASMIC SENSING, AND MUTAGENESIS OF
RP   ARG-107; HIS-110 AND ARG-147.
RC   STRAIN=K12;
RX   PubMed=12907689; DOI=10.1074/jbc.c300344200;
RA   Pappalardo L., Janausch I.G., Vijayan V., Zientz E., Junker J., Peti W.,
RA   Zweckstetter M., Unden G., Griesinger C.;
RT   "The NMR structure of the sensory domain of the membranous two-component
RT   fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.";
RL   J. Biol. Chem. 278:39185-39188(2003).
RN   [10] {ECO:0007744|PDB:3BY8}
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 42-181 IN COMPLEX WITH
RP   (R)-MALATE, DOMAIN PERIPLASMIC SENSING, AND SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=18701447; DOI=10.1074/jbc.m805253200;
RA   Cheung J., Hendrickson W.A.;
RT   "Crystal structures of C4-dicarboxylate ligand complexes with sensor
RT   domains of histidine kinases DcuS and DctB.";
RL   J. Biol. Chem. 283:30256-30265(2008).
RN   [11] {ECO:0007744|PDB:2W0N}
RP   STRUCTURE BY NMR OF 211-325, DOMAIN CYTOPLASMIC PAS, SUBUNIT, AND
RP   MUTAGENESIS OF ASN-248 AND ASN-304.
RX   PubMed=18820688; DOI=10.1038/nsmb.1493;
RA   Etzkorn M., Kneuper H., Dunnwald P., Vijayan V., Kramer J., Griesinger C.,
RA   Becker S., Unden G., Baldus M.;
RT   "Plasticity of the PAS domain and a potential role for signal transduction
RT   in the histidine kinase DcuS.";
RL   Nat. Struct. Mol. Biol. 15:1031-1039(2008).
CC   -!- FUNCTION: Member of the two-component regulatory system DcuR/DcuS
CC       (PubMed:12167640, PubMed:9765574, PubMed:9973351). Involved in the C4-
CC       dicarboxylate-stimulated regulation of the genes encoding the anaerobic
CC       fumarate respiratory system (frdABCD; nuoAN; dcuB; sdhCDAB; etc.)
CC       (PubMed:9765574, PubMed:9973351). Weakly regulates the aerobic C4-
CC       dicarboxylate transporter dctA (PubMed:9973351). Activates DcuR by
CC       phosphorylation (PubMed:12167640). {ECO:0000269|PubMed:12167640,
CC       ECO:0000269|PubMed:9765574, ECO:0000269|PubMed:9973351}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:12167640};
CC   -!- ACTIVITY REGULATION: Autophosphorylation is stimulated by the presence
CC       of C4-dicarboxylates such as fumarate or succinate (PubMed:12167640).
CC       DcuB is required for converting DcuS to the sensory competent state
CC       (PubMed:27318186). {ECO:0000269|PubMed:12167640,
CC       ECO:0000269|PubMed:27318186}.
CC   -!- SUBUNIT: Homodimer (Probable). Interacts with DctA and DcuB
CC       (PubMed:27318186). DctA/DcuS and DcuB/DcuS complexes are present both
CC       in the absence or presence of fumarate (PubMed:27318186).
CC       {ECO:0000269|PubMed:27318186, ECO:0000305|PubMed:18701447,
CC       ECO:0000305|PubMed:18820688}.
CC   -!- INTERACTION:
CC       P0AEC8; P0AEC8: dcuS; NbExp=8; IntAct=EBI-1134683, EBI-1134683;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12167640,
CC       ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DOMAIN: The periplasmic domain is involved in C4-dicarboxylate binding
CC       and sensing. The structural disorder in the cytoplasmic PAS domain has
CC       an important role in signal transduction to the kinase domain and may
CC       be the decisive structural feature that characterizes the activated
CC       kinase. {ECO:0000269|PubMed:12907689, ECO:0000269|PubMed:18701447,
CC       ECO:0000269|PubMed:18820688}.
CC   -!- PTM: Autophosphorylated (PubMed:12167640). The phosphoryl group is
CC       rapidly transferred to DcuR (PubMed:12167640).
CC       {ECO:0000269|PubMed:12167640}.
CC   -!- MISCELLANEOUS: The region encompassing approximately residues 42 to 181
CC       has been shown to be periplasmic, however exactly which residues are
CC       periplasmic is not clear.
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DR   EMBL; U14003; AAA97025.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77086.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78127.1; -; Genomic_DNA.
DR   PIR; D65222; D65222.
DR   RefSeq; NP_418549.1; NC_000913.3.
DR   RefSeq; WP_001216477.1; NZ_CP009789.1.
DR   PDB; 1OJG; NMR; -; A=45-180.
DR   PDB; 2W0N; NMR; -; A=211-325.
DR   PDB; 3BY8; X-ray; 1.45 A; A=42-181.
DR   AlphaFoldDB; P0AEC8; -.
DR   BMRB; P0AEC8; -.
DR   SMR; P0AEC8; -.
DR   BioGRID; 4261981; 14.
DR   DIP; DIP-9414N; -.
DR   FunCoup; P0AEC8; 244.
DR   IntAct; P0AEC8; 3.
DR   STRING; 511145.b4125; -.
DR   jPOST; P0AEC8; -.
DR   PaxDb; 511145-b4125; -.
DR   EnsemblBacteria; AAC77086; AAC77086; b4125.
DR   GeneID; 75169643; -.
DR   GeneID; 948639; -.
DR   KEGG; ecj:JW4086; -.
DR   KEGG; eco:b4125; -.
DR   KEGG; ecoc:C3026_22295; -.
DR   PATRIC; fig|1411691.4.peg.2575; -.
DR   EchoBASE; EB2358; -.
DR   eggNOG; COG3290; Bacteria.
DR   HOGENOM; CLU_020211_11_2_6; -.
DR   InParanoid; P0AEC8; -.
DR   OMA; HYQNGWL; -.
DR   OrthoDB; 9792686at2; -.
DR   PhylomeDB; P0AEC8; -.
DR   BioCyc; EcoCyc:DCUS-MONOMER; -.
DR   BioCyc; MetaCyc:DCUS-MONOMER; -.
DR   BRENDA; 2.7.13.3; 2165.
DR   EvolutionaryTrace; P0AEC8; -.
DR   PRO; PR:P0AEC8; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0AEC8; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR   GO; GO:0009365; C:protein histidine kinase complex; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR   GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoliWiki.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoliWiki.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:EcoliWiki.
DR   GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR   CDD; cd16915; HATPase_DpiB-CitA-like; 1.
DR   CDD; cd00130; PAS; 1.
DR   FunFam; 1.10.287.130:FF:000011; Sensor histidine kinase DcuS; 1.
DR   FunFam; 3.30.450.20:FF:000018; Sensor histidine kinase DcuS; 1.
DR   FunFam; 3.30.450.20:FF:000045; Sensor histidine kinase DcuS; 1.
DR   FunFam; 3.30.565.10:FF:000041; 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   NCBIfam; NF008298; PRK11086.1; 1.
DR   PANTHER; PTHR43547:SF10; SENSOR HISTIDINE KINASE DCUS; 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.
DR   PROSITE; PS50112; PAS; 1.
DR   PDBsum; 1OJG; -.
DR   PDBsum; 2W0N; -.
DR   PDBsum; 3BY8; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..543
FT                   /note="Sensor histidine kinase DcuS"
FT                   /id="PRO_0000074750"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..181
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        203..543
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:15919996,
FT                   ECO:0000305|PubMed:9973351"
FT   DOMAIN          212..323
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          346..538
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   BINDING         107..110
FT                   /ligand="(R)-malate"
FT                   /ligand_id="ChEBI:CHEBI:15588"
FT                   /evidence="ECO:0000269|PubMed:18701447,
FT                   ECO:0007744|PDB:3BY8"
FT   BINDING         121
FT                   /ligand="(R)-malate"
FT                   /ligand_id="ChEBI:CHEBI:15588"
FT                   /evidence="ECO:0000269|PubMed:18701447,
FT                   ECO:0007744|PDB:3BY8"
FT   BINDING         140..142
FT                   /ligand="(R)-malate"
FT                   /ligand_id="ChEBI:CHEBI:15588"
FT                   /evidence="ECO:0000269|PubMed:18701447,
FT                   ECO:0007744|PDB:3BY8"
FT   BINDING         147
FT                   /ligand="(R)-malate"
FT                   /ligand_id="ChEBI:CHEBI:15588"
FT                   /evidence="ECO:0000269|PubMed:18701447,
FT                   ECO:0007744|PDB:3BY8"
FT   MOD_RES         349
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MUTAGEN         107
FT                   /note="R->A: Abolishes the stimulation by fumarate to the
FT                   same extent as complete deletion of the dcuS gene."
FT                   /evidence="ECO:0000269|PubMed:12907689"
FT   MUTAGEN         110
FT                   /note="H->A: Abolishes the stimulation by fumarate to the
FT                   same extent as complete deletion of the dcuS gene."
FT                   /evidence="ECO:0000269|PubMed:12907689"
FT   MUTAGEN         147
FT                   /note="R->A: Abolishes the stimulation by fumarate to the
FT                   same extent as complete deletion of the dcuS gene."
FT                   /evidence="ECO:0000269|PubMed:12907689"
FT   MUTAGEN         248
FT                   /note="N->A,D,G: Causes constitutive active state of the
FT                   kinase, leading to constitutive expression of a target
FT                   gene, without addition of C4-dicarboxylates."
FT                   /evidence="ECO:0000269|PubMed:18820688"
FT   MUTAGEN         304
FT                   /note="N->D: Causes constitutive active state of the
FT                   kinase, leading to constitutive expression of a target
FT                   gene, without addition of C4-dicarboxylates."
FT                   /evidence="ECO:0000269|PubMed:18820688"
FT   HELIX           47..65
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   TURN            71..74
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   HELIX           82..92
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   HELIX           127..130
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   STRAND          134..138
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   STRAND          145..153
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:1OJG"
FT   STRAND          159..168
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   HELIX           169..177
FT                   /evidence="ECO:0007829|PDB:3BY8"
FT   HELIX           214..217
FT                   /evidence="ECO:0007829|PDB:2W0N"
FT   HELIX           221..229
FT                   /evidence="ECO:0007829|PDB:2W0N"
FT   STRAND          236..239
FT                   /evidence="ECO:0007829|PDB:2W0N"
FT   TURN            240..242
FT                   /evidence="ECO:0007829|PDB:2W0N"
FT   HELIX           249..255
FT                   /evidence="ECO:0007829|PDB:2W0N"
FT   TURN            259..263
FT                   /evidence="ECO:0007829|PDB:2W0N"
FT   HELIX           277..284
FT                   /evidence="ECO:0007829|PDB:2W0N"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:2W0N"
FT   HELIX           307..309
FT                   /evidence="ECO:0007829|PDB:2W0N"
FT   STRAND          317..319
FT                   /evidence="ECO:0007829|PDB:2W0N"
SQ   SEQUENCE   543 AA;  60551 MW;  653C369344CBA238 CRC64;
     MRHSLPYRML RKRPMKLSTT VILMVSAVLF SVLLVVHLIY FSQISDMTRD GLANKALAVA
     RTLADSPEIR QGLQKKPQES GIQAIAEAVR KRNDLLFIVV TDMQSLRYSH PEAQRIGQPF
     KGDDILKALN GEENVAINRG FLAQALRVFT PIYDENHKQI GVVAIGLELS RVTQQINDSR
     WSIIWSVLFG MLVGLIGTCI LVKVLKKILF GLEPYEISTL FEQRQAMLQS IKEGVVAVDD
     RGEVTLINDA AQELLNYRKS QDDEKLSTLS HSWSQVVDVS EVLRDGTPRR DEEITIKDRL
     LLINTVPVRS NGVIIGAIST FRDKTEVRKL MQRLDGLVNY ADALRERSHE FMNKLHVILG
     LLHLKSYKQL EDYILKTANN YQEEIGSLLG KIKSPVIAGF LISKINRATD LGHTLILNSE
     SQLPDSGSED QVATLITTLG NLIENALEAL GPEPGGEISV TLHYRHGWLH CEVNDDGPGI
     APDKIDHIFD KGVSTKGSER GVGLALVKQQ VENLGGSIAV ESEPGIFTQF FVQIPWDGER
     SNR
//