Difference between revisions of "SufS"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU32690&redirect=T BSU32690] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU32690&redirect=T BSU32690] | ||
* '''Structure:''' | * '''Structure:''' |
Revision as of 14:41, 2 April 2014
- Description: cysteine desulfurase, cysteine:SufU sulfuryl transferase
Gene name | sufS |
Synonyms | yurW, csd |
Essential | yes PubMed |
Product | cysteine desulfurase |
Function | formation of iron-sulfur clusters in proteins |
Gene expression levels in SubtiExpress: sufS | |
Interactions involving this protein in SubtInteract: SufS | |
MW, pI | 44 kDa, 5.199 |
Gene length, protein length | 1218 bp, 406 aa |
Immediate neighbours | sufU, sufD |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
iron metabolism, essential genes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU32690
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU32690
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Protein family: Csd subfamily (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Modification:
Database entries
- BsubCyc: BSU32690
- Structure:
- UniProt: O32164
- KEGG entry: [2]
- E.C. number: 2.8.1.7
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- 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
Bruna P Selbach, Alexander H Chung, Aubrey D Scott, Simon J George, Stephen P Cramer, Patricia C Dos Santos
Fe-S cluster biogenesis in Gram-positive bacteria: SufU is a zinc-dependent sulfur transfer protein.
Biochemistry: 2014, 53(1);152-60
[PubMed:24321018]
[WorldCat.org]
[DOI]
(I p)
Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849]
[WorldCat.org]
[DOI]
(I p)
Alexander G Albrecht, Florian Peuckert, Hannes Landmann, Marcus Miethke, Andreas Seubert, Mohamed A Marahiel
Mechanistic characterization of sulfur transfer from cysteine desulfurase SufS to the iron-sulfur scaffold SufU in Bacillus subtilis.
FEBS Lett: 2011, 585(3);465-70
[PubMed:21236255]
[WorldCat.org]
[DOI]
(I p)
Bruna Selbach, Emily Earles, Patricia C Dos Santos
Kinetic analysis of the bisubstrate cysteine desulfurase SufS from Bacillus subtilis.
Biochemistry: 2010, 49(40);8794-802
[PubMed:20822158]
[WorldCat.org]
[DOI]
(I p)
Alexander G Albrecht, Daili J A Netz, Marcus Miethke, Antonio J Pierik, Olaf Burghaus, Florian Peuckert, Roland Lill, Mohamed A Marahiel
SufU is an essential iron-sulfur cluster scaffold protein in Bacillus subtilis.
J Bacteriol: 2010, 192(6);1643-51
[PubMed:20097860]
[WorldCat.org]
[DOI]
(I p)