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Escherichia coli K-12 substr. MG1655 Polypeptide: DcuS sensory histidine kinase



Gene: dcuS Accession Numbers: G7827 (EcoCyc), b4125, ECK4118

Synonyms: yjdH

Regulation Summary Diagram: ?

Alternative forms of DcuS sensory histidine kinase: DcuS sensory histidine kinase - phosphorylated (summary available)

Summary:
DcuS acts as a C4-dicarboxylate-sensing histidine kinase [Zientz98, Golby99]. Its periplasmic domain reports the external C4-dicarboxylate concentration to the DcuR regulator protein [Golby99]. The chemical properties of the active DcuS ligands have been studied [Zientz98, Kneuper05].

Autophosphorylyation of DcuS is stimulated by C4-dicarboxylates, and the phosphate group is transferred to DcuR in vitro [Janausch02a, AboAmer04]. In this way, it is involved in the regulation of the genes that encode the anaerobic fumarate respiratory system (frdABCD, nuoAN, dcuB, dcuC, sdhCDAB, etc). DcuSR also increases expression of dctA to some extent [Golby99]. dcuSR belongs to the NarL regulon and is repressed by nitrate acting throught the NarXL regulatory system so that E. coli will use nitrate as a respiratory electron acceptor before fumarate [Goh05].

DcuS requires the transport proteins DctA or DcuB for normal function. DcuS interacts specifically with DctA in vivo [Witan12].

A solution structure of the periplasmic domain of DcuS has been determined [Pappalardo03]. DcuS contains two transmembrane helices flanking a periplasmic sensor domain [Taylor99a] (PASP) followed by a cytoplasmic sensor domain (PASC) and a C-terminal kinase domain [Golby99, Pappalardo03]. DcuS is present as a dimer or higher order oligomer in vivo [Scheu10]

Based on in vivo studies with fluorescence resonance energy transfer (FRET) and a bacterial two-hybrid system (BATCH), the physical interaction between DcuS and DipB sensory histidine kinase proteins has been demonstrated [Scheu12]. Such an interaction seems to have no direct functional significance and is not involved in signal transfer between the DcuSR and DipBA systems [Scheu12].

Review: [Janausch02, Witan12a, Scheu10a]

Citations: [Cheung08]

Gene Citations: [Salmon03]

Locations: inner membrane

Map Position: [4,348,054 <- 4,349,685] (93.71 centisomes)
Length: 1632 bp / 543 aa

Molecular Weight of Polypeptide: 60.551 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0013509 , EchoBASE:EB2358 , EcoGene:EG12465 , EcoliWiki:b4125 , ModBase:P0AEC8 , OU-Microarray:b4125 , PortEco:dcuS , PR:PRO_000022416 , Protein Model Portal:P0AEC8 , RegulonDB:G7827 , SMR:P0AEC8 , String:511145.b4125 , Swiss-Model:P0AEC8 , UniProt:P0AEC8

Relationship Links: InterPro:IN-FAMILY:IPR000014 , InterPro:IN-FAMILY:IPR003594 , InterPro:IN-FAMILY:IPR003661 , InterPro:IN-FAMILY:IPR004358 , InterPro:IN-FAMILY:IPR005467 , InterPro:IN-FAMILY:IPR009082 , InterPro:IN-FAMILY:IPR013767 , InterPro:IN-FAMILY:IPR016120 , PDB:Structure:1OJG , PDB:Structure:2W0N , PDB:Structure:3BY8 , Pfam:IN-FAMILY:PF00989 , Pfam:IN-FAMILY:PF02518 , Prints:IN-FAMILY:PR00344 , Prosite:IN-FAMILY:PS50109 , Prosite:IN-FAMILY:PS50112 , Smart:IN-FAMILY:SM00091 , Smart:IN-FAMILY:SM00387

In Paralogous Gene Group: 122 (29 members)

Reactions known to consume the compound:

DcuSR Two-Component Signal Transduction System, dicarboxylate-dependent :
DcuS[inner membrane] + ATP → DcuS sensory histidine kinase - phosphorylated[inner membrane] + ADP

Reactions known to produce the compound:

DcuSR Two-Component Signal Transduction System, dicarboxylate-dependent :
DcuR + DcuS sensory histidine kinase - phosphorylated[inner membrane] → DcuR-Pasp + DcuS[inner membrane]

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0000160 - phosphorelay signal transduction system Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Janausch02a]
GO:0006355 - regulation of transcription, DNA-templated Inferred from experiment Inferred by computational analysis [GOA01, AboAmer04]
GO:0006468 - protein phosphorylation Inferred from experiment [Janausch02a]
GO:0018106 - peptidyl-histidine phosphorylation Inferred by computational analysis Inferred from experiment [Janausch02a, GOA01a]
GO:0023014 - signal transduction by phosphorylation Inferred by computational analysis Inferred from experiment [Golby99, GOA01]
GO:0051260 - protein homooligomerization Inferred from experiment [Scheu10]
GO:0007165 - signal transduction Inferred by computational analysis [GOA01]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0000155 - phosphorelay sensor kinase activity Inferred from experiment Inferred by computational analysis [GOA01, Golby99]
GO:0004673 - protein histidine kinase activity Inferred from experiment Inferred by computational analysis [GOA01a, Janausch02a]
GO:0004871 - signal transducer activity Inferred from experiment Inferred by computational analysis [GOA01, Janausch02a]
GO:0042802 - identical protein binding Inferred from experiment [Scheu12, Scheu10]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016772 - transferase activity, transferring phosphorus-containing groups Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Daley05, Janausch02]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Golby99]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11, Pappalardo03]

MultiFun Terms: information transfer protein related posttranslational modification
metabolism energy metabolism, carbon anaerobic respiration
regulation type of regulation posttranscriptional covalent modification, demodification, maturation
regulation type of regulation transcriptional level complex regulation two component regulatory systems (external signal)

Essentiality data for dcuS knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Sequence Features

Feature Class Location Citations Comment State
Transmembrane-Region 21 -> 41
[UniProt09]
   
Mutagenesis-Variant 107
[Pappalardo03, UniProt11]
Alternate sequence: R → A; UniProt: Abolishes the stimulation by fumarate to the same extent as complete deletion of the dcuS gene.
 
Amino-Acid-Sites-That-Bind 107
[UniProt11]
UniProt: C4-dicarboxylate.
 
Mutagenesis-Variant 110
[Pappalardo03, UniProt11]
Alternate sequence: H → A; UniProt: Abolishes the stimulation by fumarate to the same extent as complete deletion of the dcuS gene.
 
Amino-Acid-Sites-That-Bind 110
[UniProt11]
UniProt: C4-dicarboxylate.
 
Amino-Acid-Sites-That-Bind 121
[UniProt11]
UniProt: C4-dicarboxylate; via amide nitrogen and carbonyl oxygen.
 
Protein-Segment 140 -> 142
[UniProt11]
UniProt: C4-dicarboxylate binding; Sequence Annotation Type: region of interest.
 
Mutagenesis-Variant 147
[Pappalardo03, UniProt11]
Alternate sequence: R → A; UniProt: Abolishes the stimulation by fumarate to the same extent as complete deletion of the dcuS gene.
 
Amino-Acid-Sites-That-Bind 147
[UniProt11]
UniProt: C4-dicarboxylate.
 
Transmembrane-Region 182 -> 202
[UniProt09]
   
Conserved-Region 212 -> 323
[UniProt11]
UniProt: PAS.
 
Conserved-Region 220 -> 291
[UniProt09]
UniProt: PAS;
 
Mutagenesis-Variant 248
[Etzkorn08, UniProt11]
Alternate sequence: N → G; UniProt: Causes constitutive active state of the kinase, leading to constitutive expression of a target gene, without addition of C4-dicarboxylates.
Alternate sequence: N → D; UniProt: Causes constitutive active state of the kinase, leading to constitutive expression of a target gene, without addition of C4-dicarboxylates.
Alternate sequence: N → A; UniProt: Causes constitutive active state of the kinase, leading to constitutive expression of a target gene, without addition of C4-dicarboxylates.
 
Mutagenesis-Variant 304
[Etzkorn08, UniProt11]
Alternate sequence: N → D; UniProt: Causes constitutive active state of the kinase, leading to constitutive expression of a target gene, without addition of C4-dicarboxylates.
 
Conserved-Region 346 -> 538
[UniProt09]
UniProt: Histidine kinase;
 
Phosphorylation-Modification 349
[UniProt13]
UniProt: Phosphohistidine; by autocatalysis; Non-Experimental Qualifier: by similarity.
Unmodified


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

AboAmer04: Abo-Amer AE, Munn J, Jackson K, Aktas M, Golby P, Kelly DJ, Andrews SC (2004). "DNA interaction and phosphotransfer of the C4-dicarboxylate-responsive DcuS-DcuR two-component regulatory system from Escherichia coli." J Bacteriol 186(6);1879-89. PMID: 14996819

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Cheung08: Cheung J, Hendrickson WA (2008). "Crystal structures of C4-dicarboxylate ligand complexes with sensor domains of histidine kinases DcuS and DctB." J Biol Chem 283(44);30256-65. PMID: 18701447

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Etzkorn08: Etzkorn M, Kneuper H, Dunnwald P, Vijayan V, Kramer J, Griesinger C, Becker S, Unden G, Baldus M (2008). "Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS." Nat Struct Mol Biol 15(10);1031-9. PMID: 18820688

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Goh05: Goh EB, Bledsoe PJ, Chen LL, Gyaneshwar P, Stewart V, Igo MM (2005). "Hierarchical control of anaerobic gene expression in Escherichia coli K-12: the nitrate-responsive NarX-NarL regulatory system represses synthesis of the fumarate-responsive DcuS-DcuR regulatory system." J Bacteriol 187(14);4890-9. PMID: 15995204

Golby99: Golby P, Davies S, Kelly DJ, Guest JR, Andrews SC (1999). "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 1999;181(4);1238-48. PMID: 9973351

Janausch02: Janausch IG, Zientz E, Tran QH, Kroger A, Unden G (2002). "C4-dicarboxylate carriers and sensors in bacteria." Biochim Biophys Acta 1553(1-2);39-56. PMID: 11803016

Janausch02a: Janausch IG, Garcia-Moreno I, Unden G (2002). "Function of DcuS from Escherichia coli as a fumarate-stimulated histidine protein kinase in vitro." J Biol Chem 2002;277(42);39809-14. PMID: 12167640

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kneuper05: Kneuper H, Janausch IG, Vijayan V, Zweckstetter M, Bock V, Griesinger C, Unden G (2005). "The nature of the stimulus and of the fumarate binding site of the fumarate sensor DcuS of Escherichia coli." J Biol Chem 280(21);20596-603. PMID: 15781452

Pappalardo03: Pappalardo L, Janausch IG, Vijayan V, Zientz E, Junker J, Peti W, Zweckstetter M, Unden G, Griesinger C (2003). "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(40);39185-8. PMID: 12907689

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Scheu10: Scheu PD, Liao YF, Bauer J, Kneuper H, Basche T, Unden G, Erker W (2010). "Oligomeric sensor kinase DcuS in the membrane of Escherichia coli and in proteoliposomes: chemical cross-linking and FRET spectroscopy." J Bacteriol 192(13);3474-83. PMID: 20453099

Scheu10a: Scheu PD, Kim OB, Griesinger C, Unden G (2010). "Sensing by the membrane-bound sensor kinase DcuS: exogenous versus endogenous sensing of C(4)-dicarboxylates in bacteria." Future Microbiol 5(9);1383-402. PMID: 20860483

Scheu12: Scheu PD, Witan J, Rauschmeier M, Graf S, Liao YF, Ebert-Jung A, Basche T, Erker W, Unden G (2012). "CitA/CitB two-component system regulating citrate fermentation in Escherichia coli and its relation to the DcuS/DcuR system in vivo." J Bacteriol 194(3);636-45. PMID: 22101843

Taylor99a: Taylor BL, Zhulin IB (1999). "PAS domains: internal sensors of oxygen, redox potential, and light." Microbiol Mol Biol Rev 63(2);479-506. PMID: 10357859

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Witan12: Witan J, Bauer J, Wittig I, Steinmetz PA, Erker W, Unden G (2012). "Interaction of the Escherichia coli transporter DctA with the sensor kinase DcuS: presence of functional DctA/DcuS sensor units." Mol Microbiol 85(5);846-61. PMID: 22780562

Witan12a: Witan J, Monzel C, Scheu PD, Unden G (2012). "The sensor kinase DcuS of Escherichia coli: two stimulus input sites and a merged signal pathway in the DctA/DcuS sensor unit." Biol Chem 393(11);1291-7. PMID: 23109544

Zientz98: Zientz E, Bongaerts J, Unden G (1998). "Fumarate regulation of gene expression in Escherichia coli by the DcuSR (dcuSR genes) two-component regulatory system." J Bacteriol 1998;180(20);5421-5. PMID: 9765574

Other References Related to Gene Regulation

AboAmer09: Abo-Amer AE, Altalhi AD (2009). "RpoS-independent and growth phase-dependent expression of dcuSR operon of Escherichia coli." Acta Microbiol Immunol Hung 56(3);211-27. PMID: 19789137

Oyamada07: Oyamada T, Yokoyama K, Morinaga M, Suzuki M, Makino K (2007). "Expression of Escherichia coli DcuS-R two-component regulatory system is regulated by the secondary internal promoter which is activated by CRP-cAMP." J Microbiol 45(3);234-40. PMID: 17618229


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 20, 2014, BIOCYC14A.