Sensor protein phoQ (P23837)

Identification
Name:Sensor protein phoQ
Synonyms:Not Available
Gene Name:phoQ
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Member of the two-component regulatory system phoQ/phoP involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In presence of low periplasmic Mg(2+) concentrations, phoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to phoP, which results in the expression of phoP-activated genes (PAG) and repression of phoP-repressed genes (PRG). In presence of high periplasmic Mg(2+) concentrations, acts as a protein phosphatase that dephosphorylates phospho-phoP, which results in the repression of phoP-activated genes and may lead to expression of some phoP- repressed genes. 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
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:Not Available
KEGG Pathways:
  • Cationic antimicrobial peptide (CAMP) resistance eco01503
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane
membrane part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
cation binding
ion binding
kinase activity
metal ion binding
molecular transducer activity
nucleoside binding
protein histidine kinase activity
protein kinase activity
purine nucleoside binding
signal transducer activity
transferase activity
transferase activity, transferring phosphorus-containing groups
two-component sensor activity
Process
biological regulation
cellular metabolic process
metabolic process
peptidyl-histidine phosphorylation
phosphate metabolic process
phosphorus metabolic process
phosphorylation
protein amino acid phosphorylation
regulation of biological process
regulation of cellular process
signal transduction
signal transmission
signaling process
two-component signal transduction system (phosphorelay)
Gene Properties
Blattner:b1129
Gene OrientationCounterclockwise
Centisome Percentage:25.60
Left Sequence End1187539
Right Sequence End1188999
Gene Sequence:
>1461 bp
ATGCACTCCTGGAAAAAGAAACTTGTAGTATCACAATTAGCATTGGCTTGCACTCTGGCT
ATCACCTCTCAGGCTAATGCAGCAAACTATGATACCTGGACTTATATCGATAATCCCGTT
ACAGCACTTGATTGGGATCATATGGATAAGGCAGGCACTGTAGATGGCAACTATGTAAAC
TATAGTGGTTTTGTCTATTACAACAACACCAATGGTGATTTCGATCAGTCCTTTAACGGC
GATACCGTTAACGGCACGATCTCAACCTATTATTTGAACCATGATTATGCAGACAGTACT
GCTAATCAGCTTGATATCAGTAATTCAGTGATTCACGGTTCGATTACTTCTATGCTGCCT
GGCGGTTATTATGATCGTTTTGATGCAGATGGTAATAATCTGGGTGGATATGATTTTTAC
ACTGATGCGGTTGTTGATACACACTGGCGTGATGGTGATGTTTTCACTTTGAACATTGCT
AACACTACTATTGATGATGATTATGAAGCTCTTTACTTCACTGATTCTTATAAAGATGGT
GATGTAACCAAGCACACAAATGAGACATTTGATACAAGTGAAGGCGTTGCTGTTAATCTT
GATGTAGAAAGTAACATCAATATTTCCAATAACTCCCGCGTTGCAGGTATTGCATTATCT
CAAGGTAATACTTACAACGAAACCTACACTACCGAATCTCATACTTGGGATAACAATATC
TCTGTAAAAGATTCCACAGTGACTTCGGGTTCAAATTATATCCTGGATAGCAATACTTAT
GGCAAAACTGGTCACTTTGGCAATTCTGATGAACCGAGTGATTATGCTGGCCCGGGTGAT
GTTGCAATGTCCTTTACTGCTTCAGGTTCCGACTATGCGATGAAGAACAATGTATTCCTC
AGCAATTCAACGCTGATGGGTGATGTTGCCTTTACCAGCACCTGGAATAGTAATTTTGAT
CCGAATGGTCATGATTCCAACGGTGACGGGGTGAAAGATACCAACGGGGGTTGGACTGAT
GATAGCCTCAACGTTGATGAACTAAATCTCACTCTCGATAACGGAAGCAAGTGGGTTGGT
CAGGCAATTTATAACGTTGCTGAAACGTCAGCAATGTATGATGTTGCTACAAACAGCCTT
ACTCCTGATGCAACATATGAAAACAATGACTGGAAACGTGTTGTTGATGACAAGGTCTTC
CAGAGCGGTGTATTTAACGTAGCGTTGAATAACGGTTCTGAATGGGATACTACAGGTCGT
TCCATCGTTGATACCTTGACAGTTAATAATGGTTCTCAGGTTAATGTTTCGGAATCTAAA
TTAACTTCAGATACTATCGATTTAACTAACGGTTCTTCGCTGAACATTGGTGAAGATGGC
TACGTTGATACCGATCATCTGACTATTAACTCCTACAGTACTGTTGCGTTGACCGAATCT
ACTGGGTGGGGGGCTGATTGA
Protein Properties
Pfam Domain Function:
Protein Residues:486
Protein Molecular Weight:55299
Protein Theoretical pI:6
PDB File:1ID0
Signaling Regions:
  • None
Transmembrane Regions:
  • 17-37
  • 195-215
Protein Sequence:
>Sensor protein phoQ
MKKLLRLFFPLSLRVRFLLATAAVVLVLSLAYGMVALIGYSVSFDKTTFRLLRGESNLFY
TLAKWENNKLHVELPENIDKQSPTMTLIYDENGQLLWAQRDVPWLMKMIQPDWLKSNGFH
EIEADVNDTSLLLSGDHSIQQQLQEVREDDDDAEMTHSVAVNVYPATSRMPKLTIVVVDT
IPVELKSSYMVWSWFIYVLSANLLLVIPLLWVAAWWSLRPIEALAKEVRELEEHNRELLN
PATTRELTSLVRNLNRLLKSERERYDKYRTTLTDLTHSLKTPLAVLQSTLRSLRSEKMSV
SDAEPVMLEQISRISQQIGYYLHRASMRGGTLLSRELHPVAPLLDNLTSALNKVYQRKGV
NISLDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDEHLYIVVEDDGPGI
PLSKREVIFDRGQRVDTLRPGQGVGLAVAREITEQYEGKIVAGESMLGGARMEVIFGRQH
SAPKDE
References
External Links:
ResourceLink
Uniprot ID:P23837
Uniprot Name:PHOQ_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674512
PDB ID:1ID0
Ecogene ID:EG10732
Ecocyc:EG10732
ColiBase:b1129
Kegg Gene:b1129
EchoBASE ID:EB0725
CCDB:PHOQ_ECOLI
BacMap:16129092
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • 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 186:3006-3014. Pubmed: 15126461
  • Groisman, E. A., Heffron, F., Solomon, F. (1992). "Molecular genetic analysis of the Escherichia coli phoP locus." J Bacteriol 174:486-491. Pubmed: 1530848
  • Hagiwara, D., Sugiura, M., Oshima, T., Mori, H., Aiba, H., Yamashino, T., Mizuno, T. (2003). "Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli." J Bacteriol 185:5735-5746. Pubmed: 13129944
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kasahara, M., Nakata, A., Shinagawa, H. (1992). "Molecular analysis of the Escherichia coli phoP-phoQ operon." J Bacteriol 174:492-498. Pubmed: 1729240
  • 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 181:5516-5520. Pubmed: 10464230
  • Lesley, J. A., Waldburger, C. D. (2003). "Repression of Escherichia coli PhoP-PhoQ signaling by acetate reveals a regulatory role for acetyl coenzyme A." J Bacteriol 185:2563-2570. Pubmed: 12670981
  • Marina, A., Mott, C., Auyzenberg, A., Hendrickson, W. A., Waldburger, C. D. (2001). "Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism." J Biol Chem 276:41182-41190. Pubmed: 11493605
  • 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 185:3696-3702. Pubmed: 12813061
  • 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 69:1281-1287. Pubmed: 16041131
  • 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, a. l. .. (1996). "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 3:137-155. Pubmed: 8905232
  • Regelmann, A. G., Lesley, J. A., Mott, C., Stokes, L., Waldburger, C. D. (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 184:5468-5478. Pubmed: 12218035
  • Waldburger, C. D., Sauer, R. T. (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 271:26630-26636. Pubmed: 8900137
  • Zwir, I., Shin, D., Kato, A., Nishino, K., Latifi, T., Solomon, F., Hare, J. M., Huang, H., Groisman, E. A. (2005). "Dissecting the PhoP regulatory network of Escherichia coli and Salmonella enterica." Proc Natl Acad Sci U S A 102:2862-2867. Pubmed: 15703297