SacP

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Gene name sacP
Synonyms ipa-49d
Essential no
Product trigger enzyme: sucrose-specific
phosphotransferase system, EIIBC component
Function sucrose uptake and phosphorylation,
control of SacT activity
Gene expression levels in SubtiExpress: sacP
Interactions involving this protein in SubtInteract: SacP
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 49 kDa, 7.026
Gene length, protein length 1383 bp, 461 aa
Immediate neighbours sacA, ywcJ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SacP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SacP expression.png






























Categories containing this gene/protein

phosphotransferase systems, utilization of specific carbon sources, transcription factors and their control, trigger enzyme, membrane proteins, phosphoproteins

This gene is a member of the following regulons

CcpA regulon, SacT regulon

The gene

Basic information

  • Locus tag: BSU38050

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate (according to Swiss-Prot)
  • Protein family: PTS permease, sucrose permease (Scr) family PubMed
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
    • for expression, purification of the EIIB domain in E. coli with N-terminal His-tag, in pWH844: pGP429, available in Stülke lab
    • for expression, purification of the EIIB domain in E. coli with N-terminal His-tag and thrombin cleavage site, in pGP570: pGP436, available in Stülke lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

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)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040] [WorldCat.org] [DOI] (P p)

M Arnaud, M Débarbouillé, G Rapoport, M H Saier, J Reizer
In vitro reconstitution of transcriptional antitermination by the SacT and SacY proteins of Bacillus subtilis.
J Biol Chem: 1996, 271(31);18966-72
[PubMed:8702561] [WorldCat.org] [DOI] (P p)

S L Sutrina, P Reddy, M H Saier, J Reizer
The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease.
J Biol Chem: 1990, 265(30);18581-9
[PubMed:2120236] [WorldCat.org] (P p)

M Debarbouille, M Arnaud, A Fouet, A Klier, G Rapoport
The sacT gene regulating the sacPA operon in Bacillus subtilis shares strong homology with transcriptional antiterminators.
J Bacteriol: 1990, 172(7);3966-73
[PubMed:2163394] [WorldCat.org] [DOI] (P p)

A Fouet, M Arnaud, A Klier, G Rapoport
Bacillus subtilis sucrose-specific enzyme II of the phosphotransferase system: expression in Escherichia coli and homology to enzymes II from enteric bacteria.
Proc Natl Acad Sci U S A: 1987, 84(24);8773-7
[PubMed:3122206] [WorldCat.org] [DOI] (P p)