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Escherichia coli K-12 substr. MG1655 Protein: NarQ sensory histidine kinase



Gene: narQ Accession Numbers: EG11460 (EcoCyc), b2469, ECK2464

Synonyms: nitrate/nitrite sensor kinase

Regulation Summary Diagram: ?

Subunit composition of NarQ sensory histidine kinase = [NarQ]2

Alternative forms of NarQ: NarQ sensory histidine kinase - phosphorylated

Summary:
The E.coli NarQ and NarX proteins are paralogous sensor kinases that, together with the response regulators NarP and NarL, form a complex signal transduction system which controls anaerobic respiratory gene expression in response to nitrate and nitrite.

NarQ reponds to nitrate and nitrite by autophosphorylating at a conserved histidine residue and transferring the phosphoryl group to a conserved aspartate residue of the response regulators NarL and NarP [Chiang92, Rabin93]. Studies using the purified cytoplasmic domain of NarX and NarQ suggest a differential interaction with NarL [Schroder94].

NarQ consists of two transmembrane helices, an N-terminal periplasmic domain that is responsible for signal ligand binding and a C-terminal cytoplasmic transmitter or output module [Chiang92, Stewart03].

Citations: [Chiang97, Rabin92, Noriega08]

Locations: inner membrane

Map Position: [2,583,753 -> 2,585,453] (55.69 centisomes)
Length: 1701 bp / 566 aa

Molecular Weight of Polypeptide: 63.697 kD (from nucleotide sequence)

pI: 6.63

Unification Links: ASAP:ABE-0008132 , CGSC:36333 , DIP:DIP-10318N , EchoBASE:EB1429 , EcoGene:EG11460 , EcoliWiki:b2469 , Mint:MINT-1307707 , ModBase:P27896 , OU-Microarray:b2469 , PortEco:narQ , PR:PRO_000023358 , Protein Model Portal:P27896 , RegulonDB:EG11460 , SMR:P27896 , String:511145.b2469 , UniProt:P27896

Relationship Links: InterPro:IN-FAMILY:IPR003594 , InterPro:IN-FAMILY:IPR003660 , InterPro:IN-FAMILY:IPR005467 , InterPro:IN-FAMILY:IPR011712 , InterPro:IN-FAMILY:IPR016380 , Pfam:IN-FAMILY:PF00672 , Pfam:IN-FAMILY:PF02518 , Pfam:IN-FAMILY:PF07730 , Prosite:IN-FAMILY:PS50109 , Prosite:IN-FAMILY:PS50885 , Smart:IN-FAMILY:SM00304 , Smart:IN-FAMILY:SM00387

In Paralogous Gene Group: 122 (29 members)

Reactions known to consume the compound:

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

Reactions known to produce the compound:

NarQ Two-Component Signal Transduction System, nitrate dependent :
NarQ sensory histidine kinase - phosphorylated[inner membrane] + NarP → NarQ[inner membrane] + NarP-Pasp59
NarQ sensory histidine kinase - phosphorylated[inner membrane] + NarL → NarQ[inner membrane] + NarL-Pasp59

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0000160 - phosphorelay signal transduction system Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Rabin93]
GO:0023014 - signal transduction by phosphorylation Inferred by computational analysis Inferred from experiment [Rabin93, GOA01]
GO:0071249 - cellular response to nitrate Inferred from experiment [Chiang92]
GO:0071250 - cellular response to nitrite Inferred from experiment [Rabin93]
GO:0007165 - signal transduction Inferred by computational analysis [GOA01]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a]
GO:0018106 - peptidyl-histidine phosphorylation Inferred by computational analysis [GOA01a, GOA01]
GO:0042128 - nitrate assimilation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0000155 - phosphorelay sensor kinase activity Inferred from experiment Inferred by computational analysis [GOA01, Rabin93]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0004673 - protein histidine kinase activity Inferred by computational analysis [GOA01a, GOA01]
GO:0004871 - signal transducer activity Inferred by computational analysis [GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046983 - protein dimerization activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05, Chiang92]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01, Chiang92]

MultiFun Terms: cell structure membrane
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 narQ 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 14 -> 34
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
 
Transmembrane-Region 147 -> 167
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: potential;
 
Conserved-Region 174 -> 227
[UniProt09]
UniProt: HAMP;
 
Conserved-Region 364 -> 559
[UniProt09]
UniProt: Histidine kinase;
 
Phosphorylation-Modification 370
[UniProt10a]
UniProt: Phosphohistidine; by autocatalysis; Non-Experimental Qualifier: by similarity;
Unmodified


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b2469 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11460; confirmed by SwissProt match.


References

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

Chiang92: Chiang RC, Cavicchioli R, Gunsalus RP (1992). "Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichia coli." Mol Microbiol 1992;6(14);1913-23. PMID: 1508040

Chiang97: Chiang RC, Cavicchioli R, Gunsalus RP (1997). "'Locked-on' and 'locked-off' signal transduction mutations in the periplasmic domain of the Escherichia coli NarQ and NarX sensors affect nitrate- and nitrite-dependent regulation by NarL and NarP." Mol Microbiol 1997;24(5);1049-60. PMID: 9220011

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

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.

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

Noriega08: Noriega CE, Schmidt R, Gray MJ, Chen LL, Stewart V (2008). "Autophosphorylation and dephosphorylation by soluble forms of the nitrate-responsive sensors NarX and NarQ from Escherichia coli K-12." J Bacteriol 190(11);3869-76. PMID: 18375557

Rabin92: Rabin RS, Stewart V (1992). "Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12." Proc Natl Acad Sci U S A 1992;89(18);8419-23. PMID: 1528845

Rabin93: Rabin RS, Stewart V (1993). "Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12." J Bacteriol 1993;175(11);3259-68. PMID: 8501030

Schroder94: Schroder I, Wolin CD, Cavicchioli R, Gunsalus RP (1994). "Phosphorylation and dephosphorylation of the NarQ, NarX, and NarL proteins of the nitrate-dependent two-component regulatory system of Escherichia coli." J Bacteriol 1994;176(16);4985-92. PMID: 8051011

Stewart03: Stewart V (2003). "Biochemical Society Special Lecture. Nitrate- and nitrite-responsive sensors NarX and NarQ of proteobacteria." Biochem Soc Trans 31(Pt 1);1-10. PMID: 12546643

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

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

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

Other References Related to Gene Regulation

Raghavan11: Raghavan R, Sage A, Ochman H (2011). "Genome-wide identification of transcription start sites yields a novel thermosensing RNA and new cyclic AMP receptor protein-regulated genes in Escherichia coli." J Bacteriol 193(11);2871-4. PMID: 21460078


Report Errors or Provide Feedback
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 Fri Dec 19, 2014, biocyc14.