SacC

• Description: levanase
  
  

Gene name	sacC
Synonyms
Essential	no
Product	levanase
Function	degradation of levan to fructose
Gene expression levels in SubtiExpress: sacC
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism
MW, pI	75 kDa, 6.789
Gene length, protein length	2031 bp, 677 aa
Immediate neighbours	yraA, levG
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

CcpA regulon, LevR regulon, SigL regulon

The gene

Basic information

• Locus tag: BSU27030

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans (according to Swiss-Prot)

• Protein family: glycosyl hydrolase 32 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P05656

• KEGG entry: [3]

• E.C. number: 3.2.1.80

Expression and regulation

• Operon: levD-levE-levF-levG-sacC PubMed

• Expression browser: sacC PubMed

• Sigma factor: SigL PubMed

• Regulation:
  • subject to carbon catabolite repression (CcpA, LevR) PubMed
  • induced in the presence of fructose (LevR) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • LevR: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481] [WorldCat.org] [DOI] (I p)

Original publications

Fiona Cuskin, James E Flint, Tracey M Gloster, Carl Morland, Arnaud Baslé, Bernard Henrissat, Pedro M Coutinho, Andrea Strazzulli, Alexandra S Solovyova, Gideon J Davies, Harry J Gilbert
How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity.
Proc Natl Acad Sci U S A: 2012, 109(51);20889-94
[PubMed:23213210] [WorldCat.org] [DOI] (I p)

Maria Elena Ortiz-Soto, Enrique Rudiño-Piñera, Maria Elena Rodriguez-Alegria, Agustin Lopez Munguia
Evaluation of cross-linked aggregates from purified Bacillus subtilis levansucrase mutants for transfructosylation reactions.
BMC Biotechnol: 2009, 9;68
[PubMed:19635162] [WorldCat.org] [DOI] (I e)

I Martin-Verstraete, J Stülke, A Klier, G Rapoport
Two different mechanisms mediate catabolite repression of the Bacillus subtilis levanase operon.
J Bacteriol: 1995, 177(23);6919-27
[PubMed:7592486] [WorldCat.org] [DOI] (P p)

M Débarbouillé, I Martin-Verstraete, F Kunst, G Rapoport
The Bacillus subtilis sigL gene encodes an equivalent of sigma 54 from gram-negative bacteria.
Proc Natl Acad Sci U S A: 1991, 88(20);9092-6
[PubMed:1924373] [WorldCat.org] [DOI] (P p)

M Débarbouillé, I Martin-Verstraete, A Klier, G Rapoport
The transcriptional regulator LevR of Bacillus subtilis has domains homologous to both sigma 54- and phosphotransferase system-dependent regulators.
Proc Natl Acad Sci U S A: 1991, 88(6);2212-6
[PubMed:1900939] [WorldCat.org] [DOI] (P p)

I Martin-Verstraete, M Débarbouillé, A Klier, G Rapoport
Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon.
J Mol Biol: 1990, 214(3);657-71
[PubMed:2117666] [WorldCat.org] [DOI] (P p)

I Martin, M Débarbouillé, E Ferrari, A Klier, G Rapoport
Characterization of the levanase gene of Bacillus subtilis which shows homology to yeast invertase.
Mol Gen Genet: 1987, 208(1-2);177-84
[PubMed:3112519] [WorldCat.org] [DOI] (P p)