Difference between revisions of "Hfq"
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3HSB 3HSB] (complex with an RNA aptamer) | + | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3HSB 3HSB] (complex with an RNA aptamer) {{PubMed|22053080}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31796 O31796] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O31796 O31796] | ||
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==Original publications== | ==Original publications== | ||
| − | <pubmed>12850135, 20445260 </pubmed> | + | <pubmed>12850135, 20445260 22053080 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:30, 6 November 2011
- Description: RNA chaperone
| Gene name | hfq |
| Synonyms | ymaH |
| Essential | no |
| Product | RNA chaperone |
| Function | unknown |
| MW, pI | 8 kDa, 8.698 |
| Gene length, protein length | 219 bp, 73 aa |
| Immediate neighbours | miaA, ymzC |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU17340
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: hfq family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: O31796
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation: repressed by glucose (7.7-fold) PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP22 (cat), available in the Stülke lab
- Expression vector:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original publications
Tatsuhiko Someya, Seiki Baba, Mai Fujimoto, Gota Kawai, Takashi Kumasaka, Kouji Nakamura
Crystal structure of Hfq from Bacillus subtilis in complex with SELEX-derived RNA aptamer: insight into RNA-binding properties of bacterial Hfq.
Nucleic Acids Res: 2012, 40(4);1856-67
[PubMed:22053080]
[WorldCat.org]
[DOI]
(I p)
Seiki Baba, Tatsuhiko Someya, Gota Kawai, Kouji Nakamura, Takashi Kumasaka
Expression, crystallization and preliminary crystallographic analysis of RNA-binding protein Hfq (YmaH) from Bacillus subtilis in complex with an RNA aptamer.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2010, 66(Pt 5);563-6
[PubMed:20445260]
[WorldCat.org]
[DOI]
(I p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
