Difference between revisions of "FhuD"
| Line 14: | Line 14: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || siderophore uptake | |style="background:#ABCDEF;" align="center"|'''Function''' || siderophore uptake | ||
|- | |- | ||
| − | |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=BSU33320 fhuD] |
|- | |- | ||
|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/FhuD FhuD] | |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/FhuD FhuD] | ||
| Line 26: | Line 26: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fhuB]]'', ''[[yvsH]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fhuB]]'', ''[[yvsH]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU33320 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU33320 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU33320 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:fhuD_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:fhuD_context.gif]] | ||
Revision as of 13:50, 13 May 2013
- Description: hydroxamate siderophore ABC transporter (only ferrichrome) (binding protein)
| Gene name | fhuD |
| Synonyms | |
| Essential | no |
| Product | hydroxamate siderophore ABC transporter (only ferrichrome) (binding protein) |
| Function | siderophore uptake |
| Gene expression levels in SubtiExpress: fhuD | |
| Interactions involving this protein in SubtInteract: FhuD | |
| Metabolic function and regulation of this protein in SubtiPathways: metal ion homeostasis | |
| MW, pI | 34 kDa, 9.158 |
| Gene length, protein length | 945 bp, 315 aa |
| Immediate neighbours | fhuB, yvsH |
| 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
ABC transporters, acquisition of iron, iron metabolism
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU33320
Phenotypes of a mutant
- poor growth with the xenosiderophore ferrichrome as single source of iron PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: bacterial solute-binding protein 8 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot), extracellular (signal peptide) PubMed
Database entries
- Structure:
- UniProt: P37580
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: fhuD (according to DBTBS)
- Sigma factor:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Marcus Miethke, Timo Kraushaar, Mohamed A Marahiel
Uptake of xenosiderophores in Bacillus subtilis occurs with high affinity and enhances the folding stabilities of substrate binding proteins.
FEBS Lett: 2013, 587(2);206-13
[PubMed:23220087]
[WorldCat.org]
[DOI]
(I p)
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[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)
Y Quentin, G Fichant, F Denizot
Inventory, assembly and analysis of Bacillus subtilis ABC transport systems.
J Mol Biol: 1999, 287(3);467-84
[PubMed:10092453]
[WorldCat.org]
[DOI]
(P p)
