Difference between revisions of "TreP"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU07800&redirect=T BSU07800] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU07800&redirect=T BSU07800] | ||
* '''Structure:''' | * '''Structure:''' |
Revision as of 13:12, 2 April 2014
- Description: trehalose-specific phosphotransferase system, EIIBC component of the PTS
Gene name | treP |
Synonyms | treB |
Essential | no |
Product | trehalose-specific phosphotransferase system, EIIBC component |
Function | trehalose uptake and phosphorylation |
Gene expression levels in SubtiExpress: treP | |
Interactions involving this protein in SubtInteract: TreP | |
Metabolic function and regulation of this protein in SubtiPathways: treP | |
MW, pI | 49 kDa, 8.555 |
Gene length, protein length | 1410 bp, 470 aa |
Immediate neighbours | yfkQ, treA |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
phosphotransferase systems, utilization of specific carbon sources, membrane proteins, phosphoproteins
This gene is a member of the following regulons
CcpA regulon, PhoP regulon, TreR regulon
The gene
Basic information
- Locus tag: BSU07800
Phenotypes of a mutant
Database entries
- BsubCyc: BSU07800
- DBTBS entry: no entry
- SubtiList entry: [1]
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
- BsubCyc: BSU07800
- Structure:
- UniProt: P39794
- KEGG entry: [2]
- E.C. number: 2.7.1.69
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- 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
Additional publications: PubMed
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)
Hiromi Ujiie, Tomoko Matsutani, Hisashi Tomatsu, Ai Fujihara, Chisato Ushida, Yasuhiko Miwa, Yasutaro Fujita, Hyouta Himeno, Akira Muto
Trans-translation is involved in the CcpA-dependent tagging and degradation of TreP in Bacillus subtilis.
J Biochem: 2009, 145(1);59-66
[PubMed:18977770]
[WorldCat.org]
[DOI]
(I 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)
L Bürklen, F Schöck, M K Dahl
Molecular analysis of the interaction between the Bacillus subtilis trehalose repressor TreR and the tre operator.
Mol Gen Genet: 1998, 260(1);48-55
[PubMed:9829827]
[WorldCat.org]
[DOI]
(P p)
F Schöck, M K Dahl
Analysis of DNA flanking the treA gene of Bacillus subtilis reveals genes encoding a putative specific enzyme IITre and a potential regulator of the trehalose operon.
Gene: 1996, 175(1-2);59-63
[PubMed:8917076]
[WorldCat.org]
[DOI]
(P p)
F Schöck, M K Dahl
Expression of the tre operon of Bacillus subtilis 168 is regulated by the repressor TreR.
J Bacteriol: 1996, 178(15);4576-81
[PubMed:8755887]
[WorldCat.org]
[DOI]
(P p)