SucC

• 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: sucC
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

ATP synthesis, carbon core metabolism, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

• Locus tag: BSU16090

Database entries

• BsubCyc: BSU16090

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Cofactors:

• 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

• BsubCyc: BSU16090

• Structure: 1JKJ (E. coli)

• UniProt: P80886

• KEGG entry: [3]

• E.C. number: 6.2.1.5

Additional information

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

Expression and regulation

• Operon: sucC-sucD PubMed

• Expression browser: sucC PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • RoxS: inhibition of translation and initiation of RNA degradation by RNase III PubMed

• Additional information:
  • the mRNA base-pairs with the RoxS sRNA PubMed
  • the roxS-sucC RNA duplex forms a cleavage site for RNase III PubMed
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 7352 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 44785 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 10243 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5100 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 8473 PubMed

Biological materials

• Mutant:
  • 1A1006 ( sucC::spec), available at BGSC
  • GP1134 (cat), available in Jörg Stülke's lab
  • GP791 (sucC-sucD::tet), available in Jörg Stülke's lab

• 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:

References

Sylvain Durand, Frédérique Braun, Efthimia Lioliou, Cédric Romilly, Anne-Catherine Helfer, Laurianne Kuhn, Noé Quittot, Pierre Nicolas, Pascale Romby, Ciarán Condon
A nitric oxide regulated small RNA controls expression of genes involved in redox homeostasis in Bacillus subtilis.
PLoS Genet: 2015, 11(2);e1004957
[PubMed:25643072] [WorldCat.org] [DOI] (I e)

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)