Difference between revisions of "SucC"
(→Biological materials) |
|||
Line 130: | Line 130: | ||
** 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 | ||
* '''Expression vector:''' | * '''Expression vector:''' |
Revision as of 12:01, 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
ATP synthesis, carbon core metabolism, phosphoproteins
This gene is a member of the following regulons
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:
- Inhibited by 2-oxoglutarate, ATP and NADH FEBS Letters
- GTP is not accept by the enzyme FEBS Letters
- Inhibited by 2-oxoglutarate, ATP and NADH FEBS Letters
Database entries
- 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
- Sigma factor:
- Additional information:
Biological materials
- Mutant:
- 1A1006 ( sucC::spec), PubMed, available at BGSC
- GP1134 (cat), available in Jörg Stülke's lab
- GP791 (sucCD::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:
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]
[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)