Difference between revisions of "Hfq"
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+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[RNA chaperones]]}} | ||
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+ | = This gene is a member of the following [[regulons]] = | ||
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=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 19:57, 8 December 2010
- 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
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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
- Structure: 3HSB (complex with an RNA aptamer)
- 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
Richard G Brennan, Todd M Link
Hfq structure, function and ligand binding.
Curr Opin Microbiol: 2007, 10(2);125-33
[PubMed:17395525]
[WorldCat.org]
[DOI]
(P p)
Poul Valentin-Hansen, Maiken Eriksen, Christina Udesen
The bacterial Sm-like protein Hfq: a key player in RNA transactions.
Mol Microbiol: 2004, 51(6);1525-33
[PubMed:15009882]
[WorldCat.org]
[DOI]
(P p)
Original publications