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Sensor histidine kinase DcuS (EC 2.7.13.3) (Fumarate sensor)

 DCUS_ECOLI              Reviewed;         543 AA.
P0AEC8; P39272; P76795; Q2M6H9;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
18-JUL-2018, entry version 120.
RecName: Full=Sensor histidine kinase DcuS;
EC=2.7.13.3;
AltName: Full=Fumarate sensor;
Name=dcuS; Synonyms=yjdH; OrderedLocusNames=b4125, JW4086;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7610040; DOI=10.1093/nar/23.12.2105;
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the
region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
CHARACTERIZATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=9765574;
Zientz E., Bongaerts J., Unden G.;
"Fumarate regulation of gene expression in Escherichia coli by the
DcuSR (dcuSR genes) two-component regulatory system.";
J. Bacteriol. 180:5421-5425(1998).
[5]
CHARACTERIZATION, AND TOPOLOGY.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=9973351;
Golby P., Davies S., Kelly D.J., Guest J.R., Andrews S.C.;
"Identification and characterization of a two-component sensor-kinase
and response-regulator system (DcuS-DcuR) controlling gene expression
in response to C4-dicarboxylates in Escherichia coli.";
J. Bacteriol. 181:1238-1248(1999).
[6]
CHARACTERIZATION.
STRAIN=K12 / AN387;
PubMed=12167640; DOI=10.1074/jbc.M204482200;
Janausch I.G., Garcia-Moreno I., Unden G.;
"Function of DcuS from Escherichia coli as a fumarate-stimulated
histidine protein kinase in vitro.";
J. Biol. Chem. 277:39809-39814(2002).
[7]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[8]
STRUCTURE BY NMR OF 45-180, DOMAIN PERIPLASMIC SENSING, AND
MUTAGENESIS OF ARG-107; HIS-110 AND ARG-147.
STRAIN=K12;
PubMed=12907689; DOI=10.1074/jbc.C300344200;
Pappalardo L., Janausch I.G., Vijayan V., Zientz E., Junker J.,
Peti W., Zweckstetter M., Unden G., Griesinger C.;
"The NMR structure of the sensory domain of the membranous two-
component fumarate sensor (histidine protein kinase) DcuS of
Escherichia coli.";
J. Biol. Chem. 278:39185-39188(2003).
[9]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 42-181 IN COMPLEX WITH
MALATE, DOMAIN PERIPLASMIC SENSING, AND SUBUNIT.
STRAIN=K12;
PubMed=18701447; DOI=10.1074/jbc.M805253200;
Cheung J., Hendrickson W.A.;
"Crystal structures of C4-dicarboxylate ligand complexes with sensor
domains of histidine kinases DcuS and DctB.";
J. Biol. Chem. 283:30256-30265(2008).
[10]
STRUCTURE BY NMR OF 211-325, DOMAIN CYTOPLASMIC PAS, SUBUNIT, AND
MUTAGENESIS OF ASN-248 AND ASN-304.
PubMed=18820688; DOI=10.1038/nsmb.1493;
Etzkorn M., Kneuper H., Dunnwald P., Vijayan V., Kramer J.,
Griesinger C., Becker S., Unden G., Baldus M.;
"Plasticity of the PAS domain and a potential role for signal
transduction in the histidine kinase DcuS.";
Nat. Struct. Mol. Biol. 15:1031-1039(2008).
-!- FUNCTION: Member of the two-component regulatory system DcuR/DcuS.
Involved in the C4-dicarboxylate-stimulated regulation of the
genes encoding the anaerobic fumarate respiratory system (frdABCD;
nuoAN; dcuB; dcuC; sdhCDAB; etc.). Weakly regulates the aerobic
C4-dicarboxylate transporter dctA. Activates DcuR by
phosphorylation.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine.
-!- ENZYME REGULATION: Autophosphorylation is stimulated by the
presence of C4-dicarboxylates such as fumarate, succinate, malate,
and tartrate.
-!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:18701447,
ECO:0000305|PubMed:18820688}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-1134683, EBI-1134683;
-!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
protein.
-!- DOMAIN: The periplasmic domain is involved in C4-dicarboxylate
binding and sensing. The structural disorder in the cytoplasmic
PAS domain has an important role in signal transduction to the
kinase domain and may be the decisive structural feature that
characterizes the activated kinase. {ECO:0000269|PubMed:12907689,
ECO:0000269|PubMed:18701447, ECO:0000269|PubMed:18820688}.
-!- PTM: Autophosphorylated. The phosphoryl group is rapidly
transferred to DcuR.
-!- MISCELLANEOUS: The region encompassing approximately residues 42
to 181 has been shown to be periplasmic, however exactly which
residues are periplasmic is not clear.
-----------------------------------------------------------------------
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EMBL; U14003; AAA97025.1; -; Genomic_DNA.
EMBL; U00096; AAC77086.1; -; Genomic_DNA.
EMBL; AP009048; BAE78127.1; -; Genomic_DNA.
PIR; D65222; D65222.
RefSeq; NP_418549.1; NC_000913.3.
RefSeq; WP_001216477.1; NZ_LN832404.1.
PDB; 1OJG; NMR; -; A=45-180.
PDB; 2W0N; NMR; -; A=211-325.
PDB; 3BY8; X-ray; 1.45 A; A=42-181.
PDBsum; 1OJG; -.
PDBsum; 2W0N; -.
PDBsum; 3BY8; -.
ProteinModelPortal; P0AEC8; -.
SMR; P0AEC8; -.
BioGrid; 4261981; 13.
DIP; DIP-9414N; -.
IntAct; P0AEC8; 3.
STRING; 316385.ECDH10B_4317; -.
iPTMnet; P0AEC8; -.
PaxDb; P0AEC8; -.
PRIDE; P0AEC8; -.
EnsemblBacteria; AAC77086; AAC77086; b4125.
EnsemblBacteria; BAE78127; BAE78127; BAE78127.
GeneID; 948639; -.
KEGG; ecj:JW4086; -.
KEGG; eco:b4125; -.
PATRIC; fig|1411691.4.peg.2575; -.
EchoBASE; EB2358; -.
EcoGene; EG12465; dcuS.
eggNOG; ENOG4105CEQ; Bacteria.
eggNOG; COG3290; LUCA.
HOGENOM; HOG000241936; -.
InParanoid; P0AEC8; -.
KO; K07701; -.
OMA; HYQNGWL; -.
PhylomeDB; P0AEC8; -.
BioCyc; EcoCyc:DCUS-MONOMER; -.
BRENDA; 2.7.13.3; 2026.
EvolutionaryTrace; P0AEC8; -.
PRO; PR:P0AEC8; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; ISS:EcoliWiki.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:EcoliWiki.
GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoliWiki.
GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoliWiki.
GO; GO:0051260; P:protein homooligomerization; IDA:EcoCyc.
GO; GO:0006468; P:protein phosphorylation; IDA:EcoliWiki.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoliWiki.
GO; GO:0023014; P:signal transduction by protein phosphorylation; IDA:EcoCyc.
CDD; cd00075; HATPase_c; 1.
CDD; cd00130; PAS; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
InterPro; IPR033463; sCache_3.
InterPro; IPR029151; Sensor-like_sf.
InterPro; IPR004358; Sig_transdc_His_kin-like_C.
InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00989; PAS; 1.
Pfam; PF17203; sCache_3_2; 1.
PRINTS; PR00344; BCTRLSENSOR.
SMART; SM00387; HATPase_c; 1.
SMART; SM00091; PAS; 1.
SUPFAM; SSF103190; SSF103190; 1.
SUPFAM; SSF55785; SSF55785; 1.
SUPFAM; SSF55874; SSF55874; 1.
SUPFAM; SSF55890; SSF55890; 1.
PROSITE; PS50109; HIS_KIN; 1.
PROSITE; PS50112; PAS; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
Complete proteome; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Transferase; Transmembrane;
Transmembrane helix; Two-component regulatory system.
CHAIN 1 543 Sensor histidine kinase DcuS.
/FTId=PRO_0000074750.
TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.
TRANSMEM 21 41 Helical. {ECO:0000255}.
TOPO_DOM 42 181 Periplasmic. {ECO:0000255}.
TRANSMEM 182 202 Helical. {ECO:0000255}.
TOPO_DOM 203 543 Cytoplasmic. {ECO:0000255}.
DOMAIN 212 323 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 346 538 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
REGION 140 142 C4-dicarboxylate binding.
BINDING 107 107 C4-dicarboxylate.
BINDING 110 110 C4-dicarboxylate.
BINDING 121 121 C4-dicarboxylate; via amide nitrogen and
carbonyl oxygen.
BINDING 147 147 C4-dicarboxylate.
MOD_RES 349 349 Phosphohistidine; by autocatalysis.
{ECO:0000255|PROSITE-ProRule:PRU00107}.
MUTAGEN 107 107 R->A: Abolishes the stimulation by
fumarate to the same extent as complete
deletion of the dcuS gene.
{ECO:0000269|PubMed:12907689}.
MUTAGEN 110 110 H->A: Abolishes the stimulation by
fumarate to the same extent as complete
deletion of the dcuS gene.
{ECO:0000269|PubMed:12907689}.
MUTAGEN 147 147 R->A: Abolishes the stimulation by
fumarate to the same extent as complete
deletion of the dcuS gene.
{ECO:0000269|PubMed:12907689}.
MUTAGEN 248 248 N->A,D,G: Causes constitutive active
state of the kinase, leading to
constitutive expression of a target gene,
without addition of C4-dicarboxylates.
{ECO:0000269|PubMed:18820688}.
MUTAGEN 304 304 N->D: Causes constitutive active state of
the kinase, leading to constitutive
expression of a target gene, without
addition of C4-dicarboxylates.
{ECO:0000269|PubMed:18820688}.
HELIX 47 64 {ECO:0000244|PDB:3BY8}.
HELIX 67 72 {ECO:0000244|PDB:3BY8}.
HELIX 77 79 {ECO:0000244|PDB:3BY8}.
HELIX 82 92 {ECO:0000244|PDB:3BY8}.
STRAND 96 102 {ECO:0000244|PDB:3BY8}.
STRAND 106 108 {ECO:0000244|PDB:3BY8}.
HELIX 113 115 {ECO:0000244|PDB:3BY8}.
HELIX 123 125 {ECO:0000244|PDB:3BY8}.
HELIX 127 130 {ECO:0000244|PDB:3BY8}.
STRAND 134 138 {ECO:0000244|PDB:3BY8}.
STRAND 140 143 {ECO:0000244|PDB:3BY8}.
STRAND 145 153 {ECO:0000244|PDB:3BY8}.
STRAND 155 157 {ECO:0000244|PDB:1OJG}.
STRAND 159 168 {ECO:0000244|PDB:3BY8}.
HELIX 169 177 {ECO:0000244|PDB:3BY8}.
HELIX 214 217 {ECO:0000244|PDB:2W0N}.
HELIX 221 229 {ECO:0000244|PDB:2W0N}.
STRAND 236 239 {ECO:0000244|PDB:2W0N}.
TURN 240 242 {ECO:0000244|PDB:2W0N}.
HELIX 249 255 {ECO:0000244|PDB:2W0N}.
TURN 259 263 {ECO:0000244|PDB:2W0N}.
HELIX 277 284 {ECO:0000244|PDB:2W0N}.
STRAND 294 298 {ECO:0000244|PDB:2W0N}.
STRAND 317 319 {ECO:0000244|PDB:2W0N}.
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


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