SacP

• Description: trigger enzyme: sucrose-specific phosphotransferase system, EIIBC component of the PTS
  
  

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
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 This image was kindly provided by SubtiList

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

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

Database entries

• Structure:

• UniProt: P05306

• KEGG entry: [3]

• E.C. number: 2.7.1.69

Expression and regulation

• Operon: sacP-sacA-ywdA PubMed

• Expression browser: sacP PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by sucrose (SacT) PubMed
  • repressed by glucose (CcpA)

• Regulatory mechanism:
  • SacT: binding to a RNA switch results in transcription antitermination PubMed
  • CcpA: transcription repression

• 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:

References

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)