DCUS_ECOLI
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 03-AUG-2022, entry version 144.
DE RecName: Full=Sensor histidine kinase DcuS;
DE EC=2.7.13.3;
DE AltName: Full=Fumarate sensor;
GN Name=dcuS; Synonyms=yjdH; OrderedLocusNames=b4125, JW4086;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 CHARACTERIZATION.
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 CHARACTERIZATION, 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 CHARACTERIZATION.
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].
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] {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 [9] {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 [10] {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 Involved in the C4-dicarboxylate-stimulated regulation of the genes
CC encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN;
CC dcuB; dcuC; sdhCDAB; etc.). Weakly regulates the aerobic C4-
CC dicarboxylate transporter dctA. Activates DcuR by phosphorylation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- ACTIVITY REGULATION: Autophosphorylation is stimulated by the presence
CC of C4-dicarboxylates such as fumarate, succinate, malate, and tartrate.
CC -!- SUBUNIT: Homodimer. {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; Multi-pass membrane protein.
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. The phosphoryl group is rapidly transferred to
CC DcuR.
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_SSZK01000018.1.
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 PDBsum; 1OJG; -.
DR PDBsum; 2W0N; -.
DR PDBsum; 3BY8; -.
DR AlphaFoldDB; P0AEC8; -.
DR BMRB; P0AEC8; -.
DR SMR; P0AEC8; -.
DR BioGRID; 4261981; 13.
DR DIP; DIP-9414N; -.
DR IntAct; P0AEC8; 3.
DR STRING; 511145.b4125; -.
DR jPOST; P0AEC8; -.
DR PaxDb; P0AEC8; -.
DR PRIDE; P0AEC8; -.
DR EnsemblBacteria; AAC77086; AAC77086; b4125.
DR EnsemblBacteria; BAE78127; BAE78127; BAE78127.
DR GeneID; 948639; -.
DR KEGG; ecj:JW4086; -.
DR KEGG; eco:b4125; -.
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 PhylomeDB; P0AEC8; -.
DR BioCyc; EcoCyc:DCUS-MON; -.
DR BioCyc; MetaCyc:DCUS-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR EvolutionaryTrace; P0AEC8; -.
DR PRO; PR:P0AEC8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; ISS:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IDA:EcoliWiki.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoliWiki.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
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; 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 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; SSF103190; SSF103190; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF55890; SSF55890; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
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:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..181
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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..64
FT /evidence="ECO:0007829|PDB:3BY8"
FT HELIX 67..72
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 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
