SucC

• Description: succinyl-CoA synthetase (beta subunit)
  
  

Gene name	sucC
Synonyms
Essential	no
Product	succinyl-CoA synthetase (beta subunit)
Function	TCA cycle
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU16090

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

Categories containing this gene/protein

ATP synthesis, carbon core metabolism, phosphoproteins

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:
  • Inhibited by 2-oxoglutarate, ATP and NADH FEBS Letters
    • GTP is not accept by the enzyme FEBS Letters

• Interactions:
  • Mdh-SucC PubMed
  • SucC-SucD PubMed

• Localization:

Database entries

• Structure: 1JKJ (E. coli)

• UniProt: P80886

• KEGG entry: [3]

• E.C. number: 6.2.1.5

Additional information

The enzyme is a dimer FEBS Letters

Expression and regulation

• Operon: sucC-sucD PubMed

• Sigma factor:

• Regulation: repressed by glucose (2.7-fold) (CcpA) PubMed

• Regulatory mechanism: CcpA: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

• Antibody:

References

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] [DOI] (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] [DOI] (P p)