Difference between revisions of "HprK"
| Line 14: | Line 14: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || carbon catabolite repression,<br/>phosphorylation of [[ptsH|HPr]] and [[Crh]] proteins at Ser46 | |style="background:#ABCDEF;" align="center"|'''Function''' || carbon catabolite repression,<br/>phosphorylation of [[ptsH|HPr]] and [[Crh]] proteins at Ser46 | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU35000 hprK] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/HPrK HprK] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/HPrK HprK] | ||
| Line 26: | Line 26: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[lgt]]'', ''[[nagA]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[lgt]]'', ''[[nagA]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU35000 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU35000 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU35000 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:hprK_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:hprK_context.gif]] | ||
Revision as of 13:57, 13 May 2013
| Gene name | hprK |
| Synonyms | ptsK, yvoB |
| Essential | no |
| Product | HPr kinase/ phosphorylase |
| Function | carbon catabolite repression, phosphorylation of HPr and Crh proteins at Ser46 |
| Gene expression levels in SubtiExpress: hprK | |
| Interactions involving this protein in SubtInteract: HprK | |
| Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism, Protein secretion | |
| MW, pI | 34 kDa, 4.906 |
| Gene length, protein length | 930 bp, 310 aa |
| Immediate neighbours | lgt, nagA |
| Sequences | Protein DNA Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
protein modification, transcription factors and their control
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU35000
Phenotypes of a mutant
no carbon catabolite repression
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + HPr = ADP + P-Ser-HPr (according to Swiss-Prot)
- Protein family: HPrK/P family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 1KKM (complex of Lactobacillus casei HprK with B. subtilis HPr-Ser-P), 1KKL (complex of Lactobacillus casei HprK with B. subtilis HPr)
- UniProt: O34483
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP202 (spc), GP858 (aphA3), GP82 (cat), available in Stülke lab
- Expression vector:
- for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP642, available in Stülke lab
- for expression/ purification of mutant HprK-G158A from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP650, available in Stülke lab
- for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP205, available in Stülke lab
- for expression, purification of the N-terminal in E. coli with N-terminal His-tag, in pWH844: pGP218, available in Stülke lab
- GFP fusion:
- two-hybrid system:
- Antibody: available in Stülke lab
Labs working on this gene/protein
Josef Deutscher, Paris-Grignon, France
Jörg Stülke, University of Göttingen, Germany Homepage
Wolfgang Hillen, Erlangen University, Germany Homepage
Anne Galinier, University of Marseille, France
Your additional remarks
References
Reviews
General Analysis, Physiology
Frederik M Meyer, Matthieu Jules, Felix M P Mehne, Dominique Le Coq, Jens J Landmann, Boris Görke, Stéphane Aymerich, Jörg Stülke
Malate-mediated carbon catabolite repression in Bacillus subtilis involves the HPrK/CcpA pathway.
J Bacteriol: 2011, 193(24);6939-49
[PubMed:22001508]
[WorldCat.org]
[DOI]
(I p)
Kalpana D Singh, Matthias H Schmalisch, Jörg Stülke, Boris Görke
Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources.
J Bacteriol: 2008, 190(21);7275-84
[PubMed:18757537]
[WorldCat.org]
[DOI]
(I p)
Holger Ludwig, Nicole Rebhan, Hans-Matti Blencke, Matthias Merzbacher, Jörg Stülke
Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation.
Mol Microbiol: 2002, 45(2);543-53
[PubMed:12123463]
[WorldCat.org]
[DOI]
(P p)
J Reizer, C Hoischen, F Titgemeyer, C Rivolta, R Rabus, J Stülke, D Karamata, M H Saier, W Hillen
A novel protein kinase that controls carbon catabolite repression in bacteria.
Mol Microbiol: 1998, 27(6);1157-69
[PubMed:9570401]
[WorldCat.org]
[DOI]
(P p)
A Galinier, M Kravanja, R Engelmann, W Hengstenberg, M C Kilhoffer, J Deutscher, J Haiech
New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression.
Proc Natl Acad Sci U S A: 1998, 95(4);1823-8
[PubMed:9465101]
[WorldCat.org]
[DOI]
(P p)
Structural Analysis of HPrK
Enzymatic Properties, Mutation Analysis
HprK as a Target For Antimicrobial Compounds
Helena Ramström, Maryline Bourotte, Claude Philippe, Martine Schmitt, Jacques Haiech, Jean-Jacques Bourguignon
Heterocyclic bis-cations as starting hits for design of inhibitors of the bifunctional enzyme histidine-containing protein kinase/phosphatase from Bacillus subtilis.
J Med Chem: 2004, 47(9);2264-75
[PubMed:15084125]
[WorldCat.org]
[DOI]
(P p)
