Difference between revisions of "SucC"

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* '''Regulation:''' repressed by glucose (2.7-fold) ([[CcpA]]) {{PubMed|12850135}}   
 
* '''Regulation:''' repressed by glucose (2.7-fold) ([[CcpA]]) {{PubMed|12850135}}   
  
* '''Regulatory mechanism:''' [[CcpA]]: transcription repression {{PubMed|12850135}}  
+
* '''Regulatory mechanism:'''  
 +
** [[CcpA]]: transcription repression {{PubMed|12850135}}
 +
** [[RoxS]]: inhibition of translation and initiation of RNA degradation by [[rnc|RNase III]] {{PubMed|25643072}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''
 +
** the mRNA base-pairs with the [[RoxS]] [[sRNA]] {{PubMed|25643072}}
 +
** the ''[[roxS]]-[[sucC]]'' RNA duplex forms a cleavage site for [[rnc|RNase III]] {{PubMed|25643072}}
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 7352 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 7352 {{PubMed|24696501}}
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=Biological materials =
 
=Biological materials =
 
* '''Mutant:'''
 
* '''Mutant:'''
** 1A1006 ( ''sucC''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A1006&Search=1A1006 BGSC]
+
** 1A1006 ( ''sucC''::''spec''), 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 (''[[sucC]]-[[sucD]]''::''tet''), available in [[Jörg Stülke]]'s lab
 
** GP791 (''[[sucC]]-[[sucD]]''::''tet''), available in [[Jörg Stülke]]'s lab
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=References=
 
=References=
  
<pubmed>12850135 17218307 11976317 20933603 15378759 22900538</pubmed>
+
<pubmed>12850135 17218307 11976317 20933603 15378759 22900538 25643072 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:49, 4 February 2015

  • 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
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, most abundant proteins

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
  • Modification: phosphorylation on Ser-220 PubMed
  • 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

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

  • 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

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)