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
- UniProtKB Entry
- P0DM80Swiss-Prot
- Organism
- Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
- NCBI Taxonomy ID
- 99287
- 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
- FunctionsATP binding / metal ion binding / phosphoprotein phosphatase activity / phosphorelay sensor kinase activityProcessespathogenesis / regulation of growthComponentsintegral 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
- PhoQ_Sensor (PF08918)
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P0DM80 UniProtKB Entry Name PHOQ_SALTY PDB ID(s) 1YAX, 3CGY, 3CGZ, 4UEY KEGG ID stm:STM1230 NCBI Gene ID 1252748 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Bio-Entities
Bio-Entity Type Virulence sensor histidine kinase PhoQ (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) protein primary- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Radicicol experimental unknown target Details