Difference between revisions of "SacP"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' cell membrane (according to Swiss-Prot) | + | * '''[[Localization]]:''' |
+ | ** cell membrane (according to Swiss-Prot) | ||
=== Database entries === | === Database entries === |
Revision as of 09:17, 1 November 2011
- 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
|
Contents
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
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)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P05306
- KEGG entry: [3]
- E.C. number: 2.7.1.69
Additional information
Expression and regulation
- Regulatory mechanism:
- SacT: binding to a RNA switch results in transcription antitermination PubMed
- CcpA: transcription repression
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
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)