Virulence sensor histidine kinase PhoQ

Details

Name
Virulence sensor histidine kinase PhoQ
Synonyms
  • 2.7.13.3
  • phoZ
  • Sensor histidine protein kinase/phosphatase PhoQ
Gene Name
phoQ
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Amino acid sequence
>lcl|BSEQ0051270|Virulence sensor histidine kinase PhoQ
MNKFARHFLPLSLRVRFLLATAGVVLVLSLAYGIVALVGYSVSFDKTTFRLLRGESNLFY
TLAKWENNKISVELPENLDMQSPTMTLIYDETGKLLWTQRNIPWLIKSIQPEWLKTNGFH
EIETNVDATSTLLSEDHSAQEKLKEVREDDDDAEMTHSVAVNIYPATARMPQLTIVVVDT
IPIELKRSYMVWSWFVYVLAANLLLVIPLLWIAAWWSLRPIEALAREVRELEDHHREMLN
PETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSV
SKAEPVMLEQISRISQQIGYYLHRASMRGSGVLLSRELHPVAPLLDNLISALNKVYQRKG
VNISMDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDDHLHIFVEDDGPG
IPHSKRSLVFDRGQRADTLRPGQGVGLAVAREITEQYAGQIIASDSLLGGARMEVVFGRQ
HPTQKEE
Number of residues
487
Molecular Weight
55466.19
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / metal ion binding / phosphoprotein phosphatase activity / phosphorelay sensor kinase activity
Processes
pathogenesis / regulation of growth
Components
integral component of membrane / intracellular / plasma membrane
General Function
Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. 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. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.
Specific Function
Atp binding
Pfam Domain Function
Transmembrane Regions
17-37 194-214
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0051271|Virulence sensor histidine kinase PhoQ (phoQ)
ATGAATAAATTTGCTCGCCATTTTCTGCCGCTGTCGCTGCGGGTTCGTTTTTTGCTGGCG
ACAGCCGGCGTCGTGCTGGTGCTTTCTTTGGCATATGGCATAGTGGCGCTGGTCGGCTAT
AGCGTAAGTTTTGATAAAACCACCTTTCGTTTGCTGCGCGGCGAAAGCAACCTGTTTTAT
ACCCTCGCCAAATGGGAAAATAATAAAATCAGCGTTGAGCTGCCTGAAAATCTGGACATG
CAAAGCCCGACCATGACGCTGATTTACGATGAAACGGGCAAATTATTATGGACGCAGCGC
AACATTCCCTGGCTGATTAAAAGCATTCAACCGGAATGGTTAAAAACGAACGGCTTCCAT
GAAATTGAAACCAACGTAGACGCCACCAGCACGCTGTTGAGCGAAGACCATTCCGCGCAG
GAAAAACTCAAAGAAGTACGTGAAGATGACGATGATGCCGAGATGACCCACTCGGTAGCG
GTAAATATTTATCCTGCCACGGCGCGGATGCCGCAGTTAACCATCGTGGTGGTCGATACC
ATTCCGATAGAACTAAAACGCTCCTATATGGTGTGGAGCTGGTTCGTATACGTGCTGGCC
GCCAATTTACTGTTAGTCATTCCTTTACTGTGGATCGCCGCCTGGTGGAGCTTACGCCCT
ATCGAGGCGCTGGCGCGGGAAGTCCGCGAGCTTGAAGATCATCACCGCGAAATGCTCAAT
CCGGAGACGACGCGTGAGCTGACCAGCCTTGTGCGCAACCTTAATCAACTGCTCAAAAGC
GAGCGTGAACGTTATAACAAATACCGCACGACCCTGACCGACCTGACGCACAGTTTAAAA
ACGCCGCTCGCGGTTTTGCAGAGTACGTTACGCTCTTTACGCAACGAAAAGATGAGCGTC
AGCAAAGCTGAACCGGTGATGCTGGAACAGATCAGCCGGATTTCCCAGCAGATCGGCTAT
TATCTGCATCGCGCCAGTATGCGCGGTAGCGGCGTGTTGTTAAGCCGCGAACTGCATCCC
GTCGCGCCGTTGTTAGATAACCTGATTTCTGCGCTAAATAAAGTTTATCAGCGTAAAGGG
GTGAATATCAGTATGGATATTTCACCAGAAATCAGTTTTGTCGGCGAGCAAAACGACTTT
GTCGAAGTGATGGGCAACGTACTGGACAACGCTTGTAAATATTGTCTGGAGTTTGTCGAG
ATTTCGGCTCGCCAGACCGACGATCATTTGCATATTTTCGTCGAAGATGACGGCCCAGGC
ATTCCCCACAGCAAACGTTCCCTGGTGTTTGATCGCGGTCAGCGCGCCGATACCCTACGA
CCAGGACAAGGCGTGGGGCTGGCTGTCGCGCGCGAGATTACGGAACAATACGCCGGGCAG
ATCATTGCCAGCGACAGTCTGCTCGGTGGCGCCCGTATGGAGGTCGTTTTTGGCCGACAG
CATCCCACACAGAAAGAGGAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0DM80
UniProtKB Entry NamePHOQ_SALTY
General References
  1. Miller SI, Kukral AM, Mekalanos JJ: A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proc Natl Acad Sci U S A. 1989 Jul;86(13):5054-8. [Article]
  2. McClelland M, Sanderson KE, Spieth J, Clifton SW, Latreille P, Courtney L, Porwollik S, Ali J, Dante M, Du F, Hou S, Layman D, Leonard S, Nguyen C, Scott K, Holmes A, Grewal N, Mulvaney E, Ryan E, Sun H, Florea L, Miller W, Stoneking T, Nhan M, Waterston R, Wilson RK: Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature. 2001 Oct 25;413(6858):852-6. [Article]
  3. Bearson BL, Wilson L, Foster JW: A low pH-inducible, PhoPQ-dependent acid tolerance response protects Salmonella typhimurium against inorganic acid stress. J Bacteriol. 1998 May;180(9):2409-17. [Article]
  4. Castelli ME, Garcia Vescovi E, Soncini FC: The phosphatase activity is the target for Mg2+ regulation of the sensor protein PhoQ in Salmonella. J Biol Chem. 2000 Jul 28;275(30):22948-54. [Article]
  5. Montagne M, Martel A, Le Moual H: Characterization of the catalytic activities of the PhoQ histidine protein kinase of Salmonella enterica serovar Typhimurium. J Bacteriol. 2001 Mar;183(5):1787-91. [Article]
  6. Sanowar S, Martel A, Moual HL: Mutational analysis of the residue at position 48 in the Salmonella enterica Serovar Typhimurium PhoQ sensor kinase. J Bacteriol. 2003 Mar;185(6):1935-41. [Article]
  7. Sanowar S, Le Moual H: Functional reconstitution of the Salmonella typhimurium PhoQ histidine kinase sensor in proteoliposomes. Biochem J. 2005 Sep 15;390(Pt 3):769-76. [Article]
  8. Cho US, Bader MW, Amaya MF, Daley ME, Klevit RE, Miller SI, Xu W: Metal bridges between the PhoQ sensor domain and the membrane regulate transmembrane signaling. J Mol Biol. 2006 Mar 10;356(5):1193-206. Epub 2005 Dec 27. [Article]
  9. Guarnieri MT, Zhang L, Shen J, Zhao R: The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ. J Mol Biol. 2008 May 23;379(1):82-93. doi: 10.1016/j.jmb.2008.03.036. Epub 2008 Mar 26. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03758RadicicolexperimentalunknownDetails