SufU

• Description: iron-sulfur cluster scaffold protein, receives iron from SufS, synthesis of Fe-S clusters
  
  

Gene name	sufU
Synonyms	yurV, iscU
Essential	yes PubMed
Product	iron-sulfur cluster scaffold protein
Function	synthesis of iron-sulfur clusters
Gene expression levels in SubtiExpress: sufU
Interactions involving this protein in SubtInteract: SufU
MW, pI	16 kDa, 4.713
Gene length, protein length	441 bp, 147 aa
Immediate neighbours	sufB, sufS
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

iron metabolism, essential genes

The gene

Basic information

• Locus tag: BSU32680

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: nifU family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors: zinc PubMed

• Effectors of protein activity:

• Interactions:
  • (Fra)2-SufU, requires iron PubMed
  • SufS-SufU PubMed

• Localization:

Database entries

• Structure: 2AZH

• UniProt: O32163

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: sufC-sufD-sufS-sufU-sufB PubMed

• Expression browser: sufU PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

Shashi Chillappagari, Andreas Seubert, Hein Trip, Oscar P Kuipers, Mohamed A Marahiel, Marcus Miethke
Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis.
J Bacteriol: 2010, 192(10);2512-24
[PubMed:20233928] [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)

Wenbin Qi, J A Cowan
A structural and functional homolog supports a general role for frataxin in cellular iron chemistry.
Chem Commun (Camb): 2010, 46(5);719-21
[PubMed:20087498] [WorldCat.org] [DOI] (I p)

K Kobayashi, S D Ehrlich, A Albertini, G Amati, K K Andersen, M Arnaud, K Asai, S Ashikaga, S Aymerich, P Bessieres, F Boland, S C Brignell, S Bron, K Bunai, J Chapuis, L C Christiansen, A Danchin, M Débarbouille, E Dervyn, E Deuerling, K Devine, S K Devine, O Dreesen, J Errington, S Fillinger, S J Foster, Y Fujita, A Galizzi, R Gardan, C Eschevins, T Fukushima, K Haga, C R Harwood, M Hecker, D Hosoya, M F Hullo, H Kakeshita, D Karamata, Y Kasahara, F Kawamura, K Koga, P Koski, R Kuwana, D Imamura, M Ishimaru, S Ishikawa, I Ishio, D Le Coq, A Masson, C Mauël, R Meima, R P Mellado, A Moir, S Moriya, E Nagakawa, H Nanamiya, S Nakai, P Nygaard, M Ogura, T Ohanan, M O'Reilly, M O'Rourke, Z Pragai, H M Pooley, G Rapoport, J P Rawlins, L A Rivas, C Rivolta, A Sadaie, Y Sadaie, M Sarvas, T Sato, H H Saxild, E Scanlan, W Schumann, J F M L Seegers, J Sekiguchi, A Sekowska, S J Séror, M Simon, P Stragier, R Studer, H Takamatsu, T Tanaka, M Takeuchi, H B Thomaides, V Vagner, J M van Dijl, K Watabe, A Wipat, H Yamamoto, M Yamamoto, Y Yamamoto, K Yamane, K Yata, K Yoshida, H Yoshikawa, U Zuber, N Ogasawara
Essential Bacillus subtilis genes.
Proc Natl Acad Sci U S A: 2003, 100(8);4678-83
[PubMed:12682299] [WorldCat.org] [DOI] (P p)