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



Gene: phoQ Accession Numbers: EG10732 (EcoCyc), b1129, ECK1115

Regulation Summary Diagram: ?

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

Summary:
PhoQ is the sensory histidine kinase of the PhoQP two-component signal transduction system. PhoQP regulates the expression of a varied set of genes in response to conditions of low Mg2+ and may have a role in cell survival in Mg2+ limiting environments [Kato99a, Garcia96].

PhoQ is a membrane protein that autophosphorylates in response to low environmental Mg2+ concentration and serves as a phosphoryl group donor for its cognate response regulator, the transcription factor PhoP [Kato99a]. A mutant PhoQ protein lacking the N-terminal sensor domain is unable to activate a PhoP dependent reporter gene in response to Mg2+ limitation [Regelmann02].

E. coli PhoQ sensor domain is monomeric in solution [Waldburger96]. Crystallised PhoQ sensor domain in a complex with nickel is dimeric with a salt bridge forming across the dimer interface. The physiological importance of the salt bridge to in vivo PhoQ function is suggested by mutagenesis [Cheung08].

Locations: inner membrane

Map Position: [1,187,539 <- 1,188,999] (25.6 centisomes)
Length: 1461 bp / 486 aa

Molecular Weight of Polypeptide: 55.3 kD (from nucleotide sequence), 55.0 kD (experimental) [Kasahara92 ]

Unification Links: ASAP:ABE-0003805 , CGSC:31922 , DIP:DIP-10501N , EchoBASE:EB0725 , EcoGene:EG10732 , EcoliWiki:b1129 , ModBase:P23837 , OU-Microarray:b1129 , PortEco:phoQ , PR:PRO_000023545 , Pride:P23837 , Protein Model Portal:P23837 , RegulonDB:EG10732 , SMR:P23837 , String:511145.b1129 , Swiss-Model:P23837 , UniProt:P23837

Relationship Links: InterPro:IN-FAMILY:IPR003594 , InterPro:IN-FAMILY:IPR003660 , InterPro:IN-FAMILY:IPR003661 , InterPro:IN-FAMILY:IPR004358 , InterPro:IN-FAMILY:IPR005467 , InterPro:IN-FAMILY:IPR009082 , InterPro:IN-FAMILY:IPR015014 , PDB:Structure:1ID0 , PDB:Structure:3BQ8 , PDB:Structure:3BQA , Pfam:IN-FAMILY:PF00672 , Pfam:IN-FAMILY:PF02518 , Pfam:IN-FAMILY:PF08918 , Prints:IN-FAMILY:PR00344 , Prosite:IN-FAMILY:PS50109 , Prosite:IN-FAMILY:PS50885 , Smart:IN-FAMILY:SM00387 , Smart:IN-FAMILY:SM00388

In Paralogous Gene Group: 122 (29 members)

Reactions known to consume the compound:

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

Reactions known to produce the compound:

PhoQP Two-Component Signal Transduction System, magnesium-dependent :
PhoP + PhoQ sensory histidine kinase - phosphorylated[inner membrane] → PhoP-Pasp51 + PhoQ[inner membrane]

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0000160 - phosphorelay signal transduction system Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Kato99a, Yamamoto05]
GO:0010350 - cellular response to magnesium starvation Inferred from experiment [Kato99a]
GO:0023014 - signal transduction by phosphorylation Inferred by computational analysis Inferred from experiment [Kato99a, GOA01a]
GO:0046777 - protein autophosphorylation Inferred from experiment [Yamamoto05]
GO:0007165 - signal transduction Inferred by computational analysis [GOA01a]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016311 - dephosphorylation Inferred by computational analysis [UniProtGOA11a]
GO:0018106 - peptidyl-histidine phosphorylation Inferred by computational analysis [GOA01a]
Molecular Function: GO:0000155 - phosphorelay sensor kinase activity Inferred from experiment Inferred by computational analysis [GOA01a, Kato99a]
GO:0046872 - metal ion binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Cheung08]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0004673 - protein histidine kinase activity Inferred by computational analysis [GOA01, GOA01a]
GO:0004721 - phosphoprotein phosphatase activity Inferred by computational analysis [UniProtGOA11a]
GO:0004871 - signal transducer activity Inferred by computational analysis [GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016772 - transferase activity, transferring phosphorus-containing groups Inferred by computational analysis [GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05, Kasahara92]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a, Kasahara92]

MultiFun Terms: cell structure membrane
information transfer protein related posttranslational modification
regulation type of regulation posttranscriptional covalent modification, demodification, maturation
regulation type of regulation transcriptional level complex regulation two component regulatory systems (external signal)

Inhibited by: negative feedback regulator of the PhoQP system Inferred from experiment [Lippa09, Comment 1]

Essentiality data for phoQ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 2]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 3]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 4]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 3]

Sequence Features

Feature Class Location Citations Comment State
Transmembrane-Region 17 -> 37
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
 
Mutagenesis-Variant 27
[Goldberg10, Regelmann02, UniProt11a]
Alternate sequence: V → N; UniProt: Shows Mg(2+)-dependent signaling and partial gene activation activity; when associated with A-202.
 
Mutagenesis-Variant 30
[Goldberg10, Regelmann02, UniProt11a]
Alternate sequence: L → N; UniProt: Shows Mg(2+)-dependent signaling and displays higher gene activation activity than wild-type; when associated with A-202.
 
Mutagenesis-Variant 47
[Minagawa05, Regelmann02, UniProt11]
Alternate sequence: T → L; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
 
Mutagenesis-Variant 48
[Regelmann02, UniProt11]
Alternate sequence: T → Y; UniProt: Higher activity than wild-type (with or without MgCl(2) or CaCl(2)).
Alternate sequence: T → W; UniProt: Decreased sensitivity to repression by calcium but not by magnesium.
Alternate sequence: T → F; UniProt: Decreased sensitivity to repression by calcium but not by magnesium.
Alternate sequence: T → R; UniProt: Confers less than 30% of the wild-type levels of phoQ/phoP- signaling cascade in absence of CaCl(2) or MgCl(2).
Alternate sequence: T → P; UniProt: Confers less than 30% of the wild-type levels of phoQ/phoP- signaling cascade in absence of CaCl(2) or MgCl(2).
Alternate sequence: T → L; UniProt: Confers less than 30% of the wild-type levels of phoQ/phoP- signaling cascade in absence of CaCl(2) or MgCl(2).
Alternate sequence: T → K; UniProt: Confers less than 30% of the wild-type levels of phoQ/phoP- signaling cascade in absence of CaCl(2) or MgCl(2).
Alternate sequence: T → I; UniProt: Confers less than 30% of the wild-type levels of phoQ/phoP- signaling cascade in absence of CaCl(2) or MgCl(2).
Alternate sequence: T → H; UniProt: Confers less than 30% of the wild-type levels of phoQ/phoP- signaling cascade in absence of CaCl(2) or MgCl(2).
Alternate sequence: T → G; UniProt: Confers less than 30% of the wild-type levels of phoQ/phoP- signaling cascade in absence of CaCl(2) or MgCl(2).
Alternate sequence: T → D; UniProt: Confers less than 30% of the wild-type levels of phoQ/phoP- signaling cascade in absence of CaCl(2) or MgCl(2).
Alternate sequence: T → V; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
Alternate sequence: T → S; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
Alternate sequence: T → Q; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
Alternate sequence: T → N; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
Alternate sequence: T → M; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
Alternate sequence: T → E; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
Alternate sequence: T → C; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
Alternate sequence: T → A; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
 
Mutagenesis-Variant 50
[Cheung08, Regelmann02, UniProt11a]
Alternate sequence: R → D; UniProt: Large decrease in the transcriptional activation of PhoQ- dependent genes.
 
Mutagenesis-Variant 54
[Cheung08, Regelmann02, UniProt11a]
Alternate sequence: G → D; UniProt: Very large decrease in the transcriptional activation of PhoQ- dependent genes.
 
Mutagenesis-Variant 68
[Minagawa05, Regelmann02, UniProt11]
Alternate sequence: N → L; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
 
Mutagenesis-Variant 90
[Minagawa05, Regelmann02, UniProt11]
Alternate sequence: D → A; UniProt: No significant effect (with or without MgCl(2) or CaCl(2)).
 
Mutagenesis-Variant 148 -> 154
[Regelmann02, Waldburger96, UniProt11]
Alternate sequence: EDDDDAE → QNNNNAQ; UniProt: Unable to bind divalent cations in vitro and impaired in the ability to respond to Mg(2+) deprivation in vivo.
 
Mutagenesis-Variant 149
[Minagawa05, Regelmann02, UniProt11]
Alternate sequence: D → A; UniProt: Wild-type effect concerning mgrB transcription.
 
Mutagenesis-Variant 150
[Minagawa05, Regelmann02, UniProt11]
Alternate sequence: D → I; UniProt: Wild-type effect concerning mgrB transcription.
 
Metal-Binding-Site 151
[UniProt11a]
UniProt: Divalent metal cation.
 
Mutagenesis-Variant 151
[Minagawa05, Regelmann02, UniProt11]
Alternate sequence: D → I; UniProt: Wild-type effect concerning mgrB transcription.
 
Metal-Binding-Site 152
[UniProt11a]
UniProt: Divalent metal cation.
 
Mutagenesis-Variant 152
[Minagawa05, Regelmann02, UniProt11]
Alternate sequence: D → F; UniProt: Wild-type effect concerning mgrB transcription.
 
Mutagenesis-Variant 179
[Cheung08, Minagawa05, Regelmann02, UniProt11a]
Alternate sequence: D → R; UniProt: Very large decrease in the transcriptional activation of PhoQ- dependent genes.
Alternate sequence: D → A; UniProt: Locked-on mutant defective in Mg(2+)-sensing and unable to control its phosphorylation state and phosphotransfer to phoP.
Alternate sequence: D → L; UniProt: Locked-on mutant defective in Mg(2+)-sensing and unable to control its phosphorylation state and phosphotransfer to phoP.
 
Transmembrane-Region 195 -> 215
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
 
Mutagenesis-Variant 199
[Goldberg10, Regelmann02, UniProt11a]
Alternate sequence: L → N; UniProt: Shows Mg(2+)-dependent signaling and partial gene activation activity; when associated with A-202.
 
Mutagenesis-Variant 202
[Goldberg10, Regelmann02, UniProt11a]
Alternate sequence: N → H; UniProt: Shows similar activity profile to wild-type.
Alternate sequence: N → E; UniProt: Shows similar activity profile to wild-type.
Alternate sequence: N → Q; UniProt: Shows similar activity profile to wild-type.
Alternate sequence: N → D; UniProt: Shows similar activity profile to wild-type.
Alternate sequence: N → R; UniProt: Shows similar activity profile to wild-type.
Alternate sequence: N → P; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → G; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → C; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → V; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → Y; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → W; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → F; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → M; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → L; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → I; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild- type PhoQ.
Alternate sequence: N → A; UniProt: Is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild-type PhoQ. Shows no detectable autophosphorylation. Still displays phosphatase activity. Recovers Mg(2+)-dependent signaling and partial gene activation activity; when associated with N-27 or N-199 or N-203 or N-205. Recovers Mg(2+)-dependent signaling and displays higher gene activation activity than wild-type; when associated with N- 30.
 
Amino-Acid-Site 202
[UniProt11a]
UniProt: Plays a critical role in the switching between kinase and phosphatase states; Sequence Annotation Type: site.
 
Mutagenesis-Variant 203
[Goldberg10, Regelmann02, UniProt11a]
Alternate sequence: L → N; UniProt: Shows Mg(2+)-dependent signaling and partial gene activation activity; when associated with A-202.
 
Mutagenesis-Variant 205
[Goldberg10, Regelmann02, UniProt11a]
Alternate sequence: L → N; UniProt: Shows Mg(2+)-dependent signaling and partial gene activation activity; when associated with A-202.
 
Conserved-Region 215 -> 266
[UniProt09]
UniProt: HAMP;
 
Conserved-Region 274 -> 480
[UniProt09]
UniProt: Histidine kinase;
 
Phosphorylation-Modification 277
[UniProt13]
UniProt: Phosphohistidine; by autocatalysis; Non-Experimental Qualifier: by similarity.
Unmodified
Metal-Binding-Site 385
[UniProt10a]
UniProt: Magnesium;
 
Nucleotide-Phosphate-Binding-Region 385 -> 393
[UniProt10a]
UniProt: ATP;
 
Mutagenesis-Variant 392
[Marina01, Regelmann02, UniProt11]
Alternate sequence: K → A; UniProt: 44-fold decrease in ATP affinity and 6-fold decrease in activity.
 
Nucleotide-Phosphate-Binding-Region 415 -> 420
[UniProt10a]
UniProt: ATP;
 
Mutagenesis-Variant 434
[Marina01, Regelmann02, UniProt11]
Alternate sequence: R → A; UniProt: 2-fold decrease in ATP affinity and 51-fold decrease in activity.
 
Nucleotide-Phosphate-Binding-Region 434 -> 446
[UniProt10a]
UniProt: ATP;
 
Mutagenesis-Variant 439
[Marina01, Regelmann02, UniProt11]
Alternate sequence: R → A; UniProt: 3-fold decrease in ATP affinity and 2-fold increase in activity.
 
Metal-Binding-Site 442
[UniProt10a]
UniProt: Magnesium;
 


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b1129 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10732; 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

Cheung08: Cheung J, Bingman CA, Reyngold M, Hendrickson WA, Waldburger CD (2008). "Crystal structure of a functional dimer of the PhoQ sensor domain." J Biol Chem 283(20);13762-70. PMID: 18348979

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

Garcia96: Garcia Vescovi E, Soncini FC, Groisman EA (1996). "Mg2+ as an extracellular signal: environmental regulation of Salmonella virulence." Cell 84(1);165-74. PMID: 8548821

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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Goldberg10: Goldberg SD, Clinthorne GD, Goulian M, DeGrado WF (2010). "Transmembrane polar interactions are required for signaling in the Escherichia coli sensor kinase PhoQ." Proc Natl Acad Sci U S A 107(18);8141-6. PMID: 20404199

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

Kasahara92: Kasahara M, Nakata A, Shinagawa H (1992). "Molecular analysis of the Escherichia coli phoP-phoQ operon." J Bacteriol 1992;174(2);492-8. PMID: 1729240

Kato99a: Kato A, Tanabe H, Utsumi R (1999). "Molecular characterization of the PhoP-PhoQ two-component system in Escherichia coli K-12: identification of extracellular Mg2+-responsive promoters." J Bacteriol 1999;181(17);5516-20. PMID: 10464230

Lippa09: Lippa AM, Goulian M (2009). "Feedback inhibition in the PhoQ/PhoP signaling system by a membrane peptide." PLoS Genet 5(12);e1000788. PMID: 20041203

Marina01: Marina A, Mott C, Auyzenberg A, Hendrickson WA, Waldburger CD (2001). "Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism." J Biol Chem 276(44);41182-90. PMID: 11493605

Minagawa05: Minagawa S, Okura R, Tsuchitani H, Hirao K, Yamamoto K, Utsumi R (2005). "Isolation and molecular characterization of the locked-on mutant of Mg2+ sensor PhoQ in Escherichia coli." Biosci Biotechnol Biochem 69(7);1281-7. PMID: 16041131

Regelmann02: Regelmann AG, Lesley JA, Mott C, Stokes L, Waldburger CD (2002). "Mutational analysis of the Escherichia coli PhoQ sensor kinase: differences with the Salmonella enterica serovar Typhimurium PhoQ protein and in the mechanism of Mg2+ and Ca2+ sensing." J Bacteriol 184(19);5468-78. PMID: 12218035

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt11a: 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 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."

Waldburger96: Waldburger CD, Sauer RT (1996). "Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants." J Biol Chem 1996;271(43);26630-6. PMID: 8900137

Yamamoto05: Yamamoto K, Hirao K, Oshima T, Aiba H, Utsumi R, Ishihama A (2005). "Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli." J Biol Chem 280(2);1448-56. PMID: 15522865

Other References Related to Gene Regulation

Coornaert10: Coornaert A, Lu A, Mandin P, Springer M, Gottesman S, Guillier M (2010). "MicA sRNA links the PhoP regulon to cell envelope stress." Mol Microbiol 76(2):467-79. PMID: 20345657

Coornaert13: Coornaert A, Chiaruttini C, Springer M, Guillier M (2013). "Post-transcriptional control of the Escherichia coli PhoQ-PhoP two-component system by multiple sRNAs involves a novel pairing region of GcvB." PLoS Genet 9(1);e1003156. PMID: 23300478

Eguchi04: Eguchi Y, Okada T, Minagawa S, Oshima T, Mori H, Yamamoto K, Ishihama A, Utsumi R (2004). "Signal transduction cascade between EvgA/EvgS and PhoP/PhoQ two-component systems of Escherichia coli." J Bacteriol 186(10);3006-14. PMID: 15126461

Huerta03: Huerta AM, Collado-Vides J (2003). "Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals." J Mol Biol 333(2);261-78. PMID: 14529615

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

Minagawa03: Minagawa S, Ogasawara H, Kato A, Yamamoto K, Eguchi Y, Oshima T, Mori H, Ishihama A, Utsumi R (2003). "Identification and molecular characterization of the Mg2+ stimulon of Escherichia coli." J Bacteriol 185(13);3696-702. PMID: 12813061

Monsieurs05: Monsieurs P, De Keersmaecker S, Navarre WW, Bader MW, De Smet F, McClelland M, Fang FC, De Moor B, Vanderleyden J, Marchal K (2005). "Comparison of the PhoPQ regulon in Escherichia coli and Salmonella typhimurium." J Mol Evol 60(4);462-74. PMID: 15883881

Nonaka06: Nonaka G, Blankschien M, Herman C, Gross CA, Rhodius VA (2006). "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress." Genes Dev 20(13);1776-89. PMID: 16818608

Wade06: Wade JT, Roa DC, Grainger DC, Hurd D, Busby SJ, Struhl K, Nudler E (2006). "Extensive functional overlap between sigma factors in Escherichia coli." Nat Struct Mol Biol 13(9);806-14. PMID: 16892065


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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 Sat Nov 22, 2014, biocyc14.