Sensor protein PhoQ
Details
- Name
- Sensor protein PhoQ
- Kind
- protein
- Synonyms
- 2.7.13.3
- Sensor histidine protein kinase/phosphatase PhoQ
- Gene Name
- phoQ
- UniProtKB Entry
- P23837Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0012300|Sensor protein PhoQ MKKLLRLFFPLSLRVRFLLATAAVVLVLSLAYGMVALIGYSVSFDKTTFRLLRGESNLFY TLAKWENNKLHVELPENIDKQSPTMTLIYDENGQLLWAQRDVPWLMKMIQPDWLKSNGFH EIEADVNDTSLLLSGDHSIQQQLQEVREDDDDAEMTHSVAVNVYPATSRMPKLTIVVVDT IPVELKSSYMVWSWFIYVLSANLLLVIPLLWVAAWWSLRPIEALAKEVRELEEHNRELLN PATTRELTSLVRNLNRLLKSERERYDKYRTTLTDLTHSLKTPLAVLQSTLRSLRSEKMSV SDAEPVMLEQISRISQQIGYYLHRASMRGGTLLSRELHPVAPLLDNLTSALNKVYQRKGV NISLDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDEHLYIVVEDDGPGI PLSKREVIFDRGQRVDTLRPGQGVGLAVAREITEQYEGKIVAGESMLGGARMEVIFGRQH SAPKDE
- Number of residues
- 486
- Molecular Weight
- 55299.105
- Theoretical pI
- 5.53
- GO Classification
- FunctionsATP binding / metal ion binding / phosphoprotein phosphatase activity / phosphorelay sensor kinase activityProcessescellular response to magnesium starvation / peptidyl-histidine phosphorylation / phosphorelay signal transduction system / protein autophosphorylation / signal transduction by protein phosphorylationComponentsintegral component of membrane / intracellular / plasma membrane
- General Function
- Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG (By similarity). PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, or treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues of MgrB are required for its action on PhoQ, which then acts on PhoP. Mediates magnesium influx to the cytosol by activation of mgtA. Promotes expression of the two-component regulatory system rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes.
- Specific Function
- ATP binding
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- 17-37 195-215
- Cellular Location
- Cell inner membrane
- Gene sequence
>lcl|BSEQ0012301|Sensor protein PhoQ (phoQ) ATGAAAAAATTACTGCGTCTTTTTTTCCCGCTCTCGCTGCGGGTACGTTTTCTGTTGGCA ACGGCAGCGGTAGTACTGGTGCTTTCGCTTGCCTACGGAATGGTCGCGCTGATCGGTTAT AGCGTCAGTTTCGATAAAACTACGTTTCGGCTGTTACGTGGCGAGAGCAATCTGTTCTAT ACCCTTGCGAAGTGGGAAAACAATAAGTTGCATGTCGAGTTACCCGAAAATATCGACAAG CAAAGCCCCACCATGACGCTAATTTATGATGAGAACGGGCAGCTTTTATGGGCGCAACGT GACGTGCCCTGGCTGATGAAGATGATCCAGCCTGACTGGCTGAAATCGAATGGTTTTCAT GAAATTGAAGCGGATGTTAACGATACCAGCCTCTTGCTGAGTGGAGATCATTCGATACAG CAACAGTTGCAGGAAGTGCGGGAAGATGATGACGACGCGGAGATGACCCACTCGGTGGCA GTAAACGTCTACCCGGCAACATCGCGGATGCCAAAATTAACCATTGTGGTGGTGGATACC ATTCCGGTGGAGCTAAAAAGTTCCTATATGGTCTGGAGCTGGTTTATCTATGTGCTCTCA GCCAATCTGCTGTTAGTGATCCCGCTGCTGTGGGTCGCCGCCTGGTGGAGTTTACGCCCC ATCGAAGCCCTGGCAAAAGAAGTCCGCGAACTGGAAGAACATAACCGCGAATTGCTCAAT CCAGCCACAACGCGAGAACTGACCAGTCTGGTACGAAACCTGAACCGATTGTTAAAAAGT GAACGCGAACGTTACGACAAATACCGTACGACGCTCACCGACCTGACCCATAGTCTGAAA ACGCCACTGGCGGTGCTGCAAAGTACGCTGCGTTCTCTGCGTAGTGAAAAGATGAGCGTC AGTGATGCTGAGCCGGTAATGCTGGAGCAAATCAGCCGCATTTCACAGCAAATTGGCTAC TACCTGCATCGTGCCAGTATGCGCGGCGGGACATTGCTCAGCCGCGAGCTGCATCCGGTC GCCCCACTGCTGGACAATCTCACCTCAGCGCTGAACAAAGTGTATCAACGCAAAGGGGTC AATATCTCTCTCGATATTTCGCCAGAGATCAGCTTTGTCGGTGAGCAGAACGATTTTGTC GAGGTGATGGGCAACGTGCTGGATAATGCCTGTAAATATTGCCTCGAGTTTGTCGAAATT TCTGCAAGGCAAACCGACGAGCATCTCTATATTGTGGTCGAGGATGATGGCCCCGGTATT CCATTAAGCAAGCGAGAGGTCATTTTCGACCGTGGTCAACGGGTTGATACTTTACGCCCT GGGCAAGGTGTAGGGCTGGCGGTAGCCCGCGAAATCACCGAGCAATATGAGGGTAAAATC GTCGCCGGAGAGAGCATGCTGGGCGGTGCGCGGATGGAGGTGATTTTTGGTCGCCAGCAT TCTGCGCCGAAAGATGAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P23837 UniProtKB Entry Name PHOQ_ECOLI GenBank Gene ID D90393 PDB ID(s) 1ID0, 3BQ8, 3BQA KEGG ID ecj:JW1115 NCBI Gene ID 946326 - General References
- Kasahara M, Nakata A, Shinagawa H: Molecular analysis of the Escherichia coli phoP-phoQ operon. J Bacteriol. 1992 Jan;174(2):492-8. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Groisman EA, Heffron F, Solomon F: Molecular genetic analysis of the Escherichia coli phoP locus. J Bacteriol. 1992 Jan;174(2):486-91. [Article]
- Waldburger CD, Sauer RT: 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 Oct 25;271(43):26630-6. [Article]
- Kato A, Tanabe H, Utsumi R: Molecular characterization of the PhoP-PhoQ two-component system in Escherichia coli K-12: identification of extracellular Mg2+-responsive promoters. J Bacteriol. 1999 Sep;181(17):5516-20. [Article]
- Regelmann AG, Lesley JA, Mott C, Stokes L, Waldburger CD: 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. 2002 Oct;184(19):5468-78. [Article]
- Lesley JA, Waldburger CD: Repression of Escherichia coli PhoP-PhoQ signaling by acetate reveals a regulatory role for acetyl coenzyme A. J Bacteriol. 2003 Apr;185(8):2563-70. [Article]
- Minagawa S, Ogasawara H, Kato A, Yamamoto K, Eguchi Y, Oshima T, Mori H, Ishihama A, Utsumi R: Identification and molecular characterization of the Mg2+ stimulon of Escherichia coli. J Bacteriol. 2003 Jul;185(13):3696-702. [Article]
- Hagiwara D, Sugiura M, Oshima T, Mori H, Aiba H, Yamashino T, Mizuno T: Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli. J Bacteriol. 2003 Oct;185(19):5735-46. [Article]
- Eguchi Y, Okada T, Minagawa S, Oshima T, Mori H, Yamamoto K, Ishihama A, Utsumi R: Signal transduction cascade between EvgA/EvgS and PhoP/PhoQ two-component systems of Escherichia coli. J Bacteriol. 2004 May;186(10):3006-14. [Article]
- Minagawa S, Okura R, Tsuchitani H, Hirao K, Yamamoto K, Utsumi R: Isolation and molecular characterization of the locked-on mutant of Mg2+ sensor PhoQ in Escherichia coli. Biosci Biotechnol Biochem. 2005 Jul;69(7):1281-7. [Article]
- Zwir I, Shin D, Kato A, Nishino K, Latifi T, Solomon F, Hare JM, Huang H, Groisman EA: Dissecting the PhoP regulatory network of Escherichia coli and Salmonella enterica. Proc Natl Acad Sci U S A. 2005 Feb 22;102(8):2862-7. Epub 2005 Feb 9. [Article]
- Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G: Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005 May 27;308(5726):1321-3. [Article]
- Lippa AM, Goulian M: Feedback inhibition in the PhoQ/PhoP signaling system by a membrane peptide. PLoS Genet. 2009 Dec;5(12):e1000788. doi: 10.1371/journal.pgen.1000788. Epub 2009 Dec 24. [Article]
- Lippa AM, Goulian M: Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli. J Bacteriol. 2012 Mar;194(6):1457-63. doi: 10.1128/JB.06055-11. Epub 2012 Jan 20. [Article]
- Goldberg SD, Clinthorne GD, Goulian M, DeGrado WF: Transmembrane polar interactions are required for signaling in the Escherichia coli sensor kinase PhoQ. Proc Natl Acad Sci U S A. 2010 May 4;107(18):8141-6. doi: 10.1073/pnas.1003166107. Epub 2010 Apr 19. [Article]
- Marina A, Mott C, Auyzenberg A, Hendrickson WA, Waldburger CD: Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism. J Biol Chem. 2001 Nov 2;276(44):41182-90. Epub 2001 Aug 7. [Article]
- Cheung J, Bingman CA, Reyngold M, Hendrickson WA, Waldburger CD: Crystal structure of a functional dimer of the PhoQ sensor domain. J Biol Chem. 2008 May 16;283(20):13762-70. doi: 10.1074/jbc.M710592200. Epub 2008 Mar 18. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Phosphoaminophosphonic Acid-Adenylate Ester experimental unknown target Details