Difference between revisions of "SucC"

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(Biological materials)
(Biological materials)
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** 1A1006 ( ''sucC''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A1006&Search=1A1006 BGSC]
 
** 1A1006 ( ''sucC''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A1006&Search=1A1006 BGSC]
 
** GP1134 (cat), available in [[Jörg Stülke]]'s lab
 
** GP1134 (cat), available in [[Jörg Stülke]]'s lab
** GP791 (''sucCD''::''tet'')available in [[Jörg Stülke]]'s lab
+
** GP791 (''sucCD''::''tet''), available in [[Jörg Stülke]]'s lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 13:01, 13 August 2013

  • Description: succinyl-CoA synthetase (beta subunit)

Gene name sucC
Synonyms
Essential no
Product succinyl-CoA synthetase (beta subunit)
Function TCA cycle
Gene expression levels in SubtiExpress: sucC
Interactions involving this protein in SubtInteract: SucC
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 41 kDa, 4.846
Gene length, protein length 1155 bp, 385 aa
Immediate neighbours ylqH, sucD
Sequences Protein DNA DNA_with_flanks
Genetic context
SucC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SucC expression.png















Categories containing this gene/protein

ATP synthesis, carbon core metabolism, phosphoproteins

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

  • Locus tag: BSU16090

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + succinate + CoA = ADP + phosphate + succinyl-CoA (according to Swiss-Prot)
  • Protein family: ATP-grasp domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Reversible Michaelis-Menten FEBS Letters
  • Domains:
  • Modification: phosphorylation on Ser-220 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1JKJ (E. coli)
  • KEGG entry: [3]

Additional information

  • extensive information on the structure and enzymatic properties of succinyl-CoA synthetase can be found at Proteopedia

Expression and regulation

  • Sigma factor:
  • Regulation: repressed by glucose (2.7-fold) (CcpA) PubMed
  • Regulatory mechanism: CcpA: transcription repression PubMed
  • Additional information:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Frederik M Meyer, Jan Gerwig, Elke Hammer, Christina Herzberg, Fabian M Commichau, Uwe Völker, Jörg Stülke
Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: evidence for a metabolon.
Metab. Eng.: 2011, 13(1);18-27
[PubMed:20933603] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol. Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab. Eng.: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] (P p)

Ciarán Condon, Jordi Rourera, Dominique Brechemier-Baey, Harald Putzer
Ribonuclease M5 has few, if any, mRNA substrates in Bacillus subtilis.
J. Bacteriol.: 2002, 184(10);2845-9
[PubMed:11976317] [WorldCat.org] (P p)