SdhC

• Description: succinate dehydrogenase(cytochrome b558 subunit)
  
  

Gene name	sdhC
Synonyms
Essential	no
Product	succinate dehydrogenase (cytochrome b558 subunit)
Function	TCA cycle
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	22 kDa, 9.831
Gene length, protein length	606 bp, 202 aa
Immediate neighbours	yslB, sdhA
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: BSU28450

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: cytochrome b558 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
• Cofactor(s): Fe

• Effectors of protein activity:
  • Inhibited by 2-(n-Heptyl)-4-hydroxy-quinoline N-oxide PubMed
  • Activated by Cytochrome b558 PubMed

• Interactions: SdhA-SdhB-SdhC

• Localization: cell membrane (according to Swiss-Prot), membrane protein PubMed

Database entries

• Structure: 1NEK (E. coli)

• Swiss prot entry: P08064

• KEGG entry: [3]

• E.C. number: 1.3.99.1

Additional information

This enzyme is a trimer membrane-bound PubMed PubMed

• One subunit is bound to citochrome b558, and this subunit is the one bound to the cytosolic side of the membrane PubMed PubMed
• Another subunit is the flavoprotein one, required for FAD usage PubMed PubMed
• The other subunit has an iron-sulphur domain necessary for the catalytic activity PubMed PubMed

Expression and regulation

• Operon: sdhC-sdhA-sdhB PubMed

• Sigma factor: SigA PubMed

• Regulation: SdhC is less expressed under conditions of extreme iron starvation (FsrA) PubMed

• Regulatory mechanism: FsrA: translational repression, sRNA PubMed

• Additional information:

Biological materials

• Mutant: GP743 (sdhCA, cat), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Ahmed Gaballa, Haike Antelmann, Claudio Aguilar, Sukhjit K Khakh, Kyung-Bok Song, Gregory T Smaldone, John D Helmann
The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins.
Proc Natl Acad Sci U S A: 2008, 105(33);11927-32
[PubMed:18697947] [WorldCat.org] [DOI] (I p)

S T Cole, C Condon, B D Lemire, J H Weiner
Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli.
Biochim Biophys Acta: 1985, 811(4);381-403
[PubMed:3910107] [WorldCat.org] [DOI] (P p)

L Hederstedt, L Rutberg
Succinate dehydrogenase--a comparative review.
Microbiol Rev: 1981, 45(4);542-55
[PubMed:6799760] [WorldCat.org] [DOI] (P p)

1. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
2. Gaballa A, Antelmann H, Aguilar C, Khakh SK, Song KB, Smaldone GT, Helmann JD (2008) The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins. PNAS 105: 11927-11932. PubMed
3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed