Difference between revisions of "SacX"
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{{SubtiWiki category|[[phosphotransferase systems]]}}, | {{SubtiWiki category|[[phosphotransferase systems]]}}, | ||
{{SubtiWiki category|[[utilization of specific carbon sources]]}}, | {{SubtiWiki category|[[utilization of specific carbon sources]]}}, | ||
+ | {{SubtiWiki category|[[transcription factors and their control]]}}, | ||
{{SubtiWiki category|[[trigger enzyme]]}}, | {{SubtiWiki category|[[trigger enzyme]]}}, | ||
{{SubtiWiki category|[[membrane proteins]]}}, | {{SubtiWiki category|[[membrane proteins]]}}, |
Revision as of 10:54, 23 April 2011
- Description: trigger enzyme: sucrose-specific phosphotransferase system, EIIBC component of the PTS (low affinity) and control of SacY activity
Gene name | sacX |
Synonyms | ipa-14r, sacS |
Essential | no |
Product | trigger enzyme: sucrose-specific phosphotransferase system, EIIBC component (low affinity) |
Function | sucrose uptake and phosphorylation, control of SacY activity |
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
MW, pI | 48 kDa, 9.346 |
Gene length, protein length | 1377 bp, 459 aa |
Immediate neighbours | epr, sacY |
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: BSU38410
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:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P15400
- KEGG entry: [3]
- E.C. number: 2.7.1.69
Additional information
Expression and regulation
- Regulation: induction by sucrose (at high concentration) PubMed
- Regulatory mechanism:
- induction by SacY-dependent RNA switch (transcriptional antitermination) PubMed
- DegU-P: transcription activation PubMed
- 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
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)
P Tortosa, D Le Coq
A ribonucleic antiterminator sequence (RAT) and a distant palindrome are both involved in sucrose induction of the Bacillus subtilis sacXY regulatory operon.
Microbiology (Reading): 1995, 141 ( Pt 11);2921-7
[PubMed:8535520]
[WorldCat.org]
[DOI]
(P p)
A M Crutz, M Steinmetz
Transcription of the Bacillus subtilis sacX and sacY genes, encoding regulators of sucrose metabolism, is both inducible by sucrose and controlled by the DegS-DegU signalling system.
J Bacteriol: 1992, 174(19);6087-95
[PubMed:1400159]
[WorldCat.org]
[DOI]
(P p)
M M Zukowski, L Miller, P Cosgwell, K Chen, S Aymerich, M Steinmetz
Nucleotide sequence of the sacS locus of Bacillus subtilis reveals the presence of two regulatory genes.
Gene: 1990, 90(1);153-5
[PubMed:2116367]
[WorldCat.org]
[DOI]
(P p)
A M Crutz, M Steinmetz, S Aymerich, R Richter, D Le Coq
Induction of levansucrase in Bacillus subtilis: an antitermination mechanism negatively controlled by the phosphotransferase system.
J Bacteriol: 1990, 172(2);1043-50
[PubMed:2105292]
[WorldCat.org]
[DOI]
(P p)