Difference between revisions of "Fur"
(→References) |
|||
Line 128: | Line 128: | ||
=References= | =References= | ||
− | + | <pubmed> 19508286 , 12354229, 16672620, 19508285 ,</pubmed> | |
− | + | ||
# Gaballa A, Antelmann H, Aguilar C, Khakh SK, Song KB, Smaldone GT, Helmann JD (2008) The ''Bacillus subtilis'' iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins. PNAS 105: 11927-11932. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Gaballa A, Antelmann H, Aguilar C, Khakh SK, Song KB, Smaldone GT, Helmann JD (2008) The ''Bacillus subtilis'' iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins. PNAS 105: 11927-11932. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] |
Revision as of 12:14, 12 June 2009
- Description: transcription regulator of iron homoeostasis
Gene name | fur |
Synonyms | yqkL |
Essential | no |
Product | transcriptional repressor |
Function | regulation of iron homoeostasis
and transcription of ferri-siderophore uptake genes |
MW, pI | 17 kDa, 5.374 |
Gene length, protein length | 447 bp, 149 aa |
Immediate neighbours | ripX, spoIIM |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU23520
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: Fur family (according to Swiss-Prot)
Genes controlled by Fur
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- Swiss prot entry: P54574
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: fur
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
John Helmann, Cornell University, USA Homepage
Your additional remarks
References
David P Giedroc
Hydrogen peroxide sensing in Bacillus subtilis: it is all about the (metallo)regulator.
Mol Microbiol: 2009, 73(1);1-4
[PubMed:19508286]
[WorldCat.org]
[DOI]
(I p)
L Jacquamet, D A K Traoré, J-L Ferrer, O Proux, D Testemale, J-L Hazemann, E Nazarenko, A El Ghazouani, C Caux-Thang, V Duarte, J-M Latour
Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding.
Mol Microbiol: 2009, 73(1);20-31
[PubMed:19508285]
[WorldCat.org]
[DOI]
(I p)
Juliane Ollinger, Kyung-Bok Song, Haike Antelmann, Michael Hecker, John D Helmann
Role of the Fur regulon in iron transport in Bacillus subtilis.
J Bacteriol: 2006, 188(10);3664-73
[PubMed:16672620]
[WorldCat.org]
[DOI]
(P p)
Noel Baichoo, Tao Wang, Rick Ye, John D Helmann
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon.
Mol Microbiol: 2002, 45(6);1613-29
[PubMed:12354229]
[WorldCat.org]
[DOI]
(P p)
- Gaballa A, Antelmann H, Aguilar C, Khakh SK, Song KB, Smaldone GT, Helmann JD (2008) The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins. PNAS 105: 11927-11932. PubMed