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| * '''Description:''' HPr kinase/ phosphorylase<br/><br/>
| | {{#bank: HprK}} |
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| {| align="right" border="1" cellpadding="2"
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| |style="background:#ABCDEF;" align="center"|'''Gene name'''
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| |''hprK''
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| |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''ptsK, yvoB ''
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| |style="background:#ABCDEF;" align="center"| '''Essential''' ||
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| |style="background:#ABCDEF;" align="center"| '''Product''' || HPr kinase/ phosphorylase
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| |style="background:#ABCDEF;" align="center"|'''Function''' || phosphorylation of HPr and Crh proteins at Ser46
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| |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 34 kDa, 4.906
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| |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 930 bp, 310 aa
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| |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' ||
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| |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/hprK_nucleotide.txt Gene sequence (+200bp) ]'''
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| |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/hprK_protein.txt Protein sequence]'''
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| |colspan="2" | '''Genetic context''' <br/> [[Image:hprK_context.gif]]
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| |}
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| __TOC__
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| <br/><br/>
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| =The gene=
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| === Basic information ===
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| * '''Coordinates:'''
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| ===Phenotypes of a mutant ===
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| no carbon catabolite repression
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| === Database entries ===
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| * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/hprK.html]
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| * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG14125]
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| === Additional information===
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| =The protein=
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| === Basic information/ Evolution ===
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| * '''Catalyzed reaction/ biological activity:'''
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| * '''Protein family:'''
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| * '''Paralogous protein(s):'''
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| === Extended information on the protein ===
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| * '''Kinetic information:'''
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| * '''Domains:'''
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| * '''Modification:'''
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| * '''Cofactor(s):'''
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| * '''Effectors of protein activity:'''
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| * '''Interactions:''' HprK-[[PtsH| HPr]], HprK-[[Crh]]
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| * '''Localization:'''
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| === Database entries ===
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| * '''Structure:'''
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| * '''Swiss prot entry:'''
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| * '''KEGG entry:'''
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| * '''E.C. number:'''
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| === Additional information===
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| =Expression and regulation=
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| * '''Operon:'''
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| * '''Sigma factor:'''
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| * '''Regulation:'''
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| * '''Regulatory mechanism:'''
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| * '''Additional information:'''
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| =Biological materials =
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| * '''Mutant:'''
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| * '''Expression vector:'''
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| * '''lacZ fusion:'''
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| * '''GFP fusion:'''
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| * '''two-hybrid system:'''
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| * '''Antibody:'''
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| =Labs working on this gene/protein=
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| [[Josef Deutscher]], Paris-Grignon, France
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| [[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
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| [[Wolfgang Hillen]], Erlangen University, Germany [http://www.biologie.uni-erlangen.de/mibi/index2.html Homepage]
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| [[Anne Galinier]], University of Marseille, France
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| =Your additional remarks=
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| =References=
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| # Reizer, J., Hoischen, C., Titgemeyer, F., Rivolta, C., Rabus, R., Stülke, J., Karamata, D., Saier, M. H., Jr., & Hillen, W. (1998) A novel bacterial protein kinase that controls carbon catabolite repression. Mol. Microbiol. 27: 1157-1169. [http://www.ncbi.nlm.nih.gov/sites/entrez/9570401 PubMed]
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| # Galinier A, Kravanja M, Engelmann R, Hengstenberg W, Kilhoffer MC, Deutscher J, Haiech J (1998) New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression. Proc Natl Acad Sci USA 95:1823-1828. [http://www.ncbi.nlm.nih.gov/sites/entrez/9465101 PubMed]
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| # Mijakovic I, Poncet S, Galiner A, Monedero V, Fieulaine S, Janin J, Nessler S, Marquez JA, Scheffzek K, Hasenbein S, Hengstenberg W, Deutscher J: Pyrophosphate-producing protein dephosphorylation by HPr kinase/ phosphorylase: a relic of early life? Proc Natl Acad Sci USA 2002, 99:13442-13447. [http://www.ncbi.nlm.nih.gov/sites/entrez/12359880 PubMed]
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| # Hanson K. G., Steinhauer, K., Reizer, J., Hillen, W. & Stülke, J. (2002) HPr kinase/phosphatase of Bacillus subtilis: Expression of the gene and effects of mutations on enzyme activity, growth, and carbon catabolite repression. Microbiology 148: 1805-1811. [http://www.ncbi.nlm.nih.gov/sites/entrez/12055300 PubMed]
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| # Jault J M, Fieulaine S, Nessler S, Gonzalo P, Di Pietro A, Deutscher J, Galinier A (2000) The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding. J Biol Chem 275:1773-1780. [http://www.ncbi.nlm.nih.gov/sites/entrez/10636874 PubMed]
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| # Ramström H, Sanglier S, Leize-Wagner E, Philippe C, van Dorsselaer A, Haiech J (2003) Properties and regulation of the bifunctional enzyme HPr kinase/phosphatase in Bacillus subtilis. J Biol Chem 278:1174-1185. [http://www.ncbi.nlm.nih.gov/sites/entrez/12411438 PubMed]
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| # Nessler S, Fieulaine S, Poncet S, Galinier A, Deutscher J, Janin J (2003) HPr kinase/phosphorylase, the sensor enzyme of catabolite repression in Gram-positive bacteria: structural aspects of the enzyme and the complex with its protein substrate. J Bacteriol 185:4003-4010. [http://www.ncbi.nlm.nih.gov/sites/entrez/12837773 PubMed]
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| # Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M. & Stülke, J. (2002) Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation. Mol. Microbiol. 45: 543-553. [http://www.ncbi.nlm.nih.gov/sites/entrez/12123463 PubMed]
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| # Singh, K. D., Schmalisch, M. H., Stülke, J. & Görke, B. (2008) Carbon catabolite repression in Bacillus subtilis: A quantitative analysis of repression exerted by different carbon sources. J. Bacteriol. 190: 7275-7284. [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537 PubMed]
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| # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
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