Difference between revisions of "LicA"
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| − | * '''Description:''' lichenan-specific phosphotransferase system, EIIA component <br/><br/> | + | * '''Description:''' lichenan-specific [[PTS|phosphotransferase system]], EIIA component of the [[PTS]]<br/><br/> |
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''Product''' || lichenan-specific phosphotransferase system, <br/>EIIA component | + | |style="background:#ABCDEF;" align="center"| '''Product''' || lichenan-specific [[PTS|phosphotransferase system]], <br/>EIIA component |
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || lichenan uptake and phosphorylation | |style="background:#ABCDEF;" align="center"|'''Function''' || lichenan uptake and phosphorylation | ||
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* '''Catalyzed reaction/ biological activity:''' Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine (according to Swiss-Prot) | * '''Catalyzed reaction/ biological activity:''' Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine (according to Swiss-Prot) | ||
| − | * '''Protein family:''' PTS permease, lactose permease (Lac) family [http://www.ncbi.nlm.nih.gov/pubmed/10627040 PubMed] | + | * '''Protein family:''' [[PTS]] permease, lactose permease (Lac) family [http://www.ncbi.nlm.nih.gov/pubmed/10627040 PubMed] |
* '''Paralogous protein(s):''' | * '''Paralogous protein(s):''' | ||
Revision as of 19:29, 24 November 2009
- Description: lichenan-specific phosphotransferase system, EIIA component of the PTS
| Gene name | licA |
| Synonyms | celC |
| Essential | no |
| Product | lichenan-specific phosphotransferase system, EIIA component |
| Function | lichenan uptake and phosphorylation |
| Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
| MW, pI | 12 kDa, 4.641 |
| Gene length, protein length | 330 bp, 110 aa |
| Immediate neighbours | licH, licC |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU38570
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 3K1S (IIA(Cel) from B. anthracis, 42% identity)
- UniProt: P46319
- KEGG entry: [2]
- E.C. number: 2.7.1.69
Additional information
Expression and regulation
- Regulation: repressed by glucose (CcpA) , carbon catabolite repression, induction by oligomeric ß-glucosides PubMed
- Regulatory mechanism: CcpA: transcription repression, catabolite repression: repression by CcpA, induction: transcription activation by the PRD-type regulator LicR 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
Takashi Inaoka, Takenori Satomura, Yasutaro Fujita, Kozo Ochi
Novel gene regulation mediated by overproduction of secondary metabolite neotrehalosadiamine in Bacillus subtilis.
FEMS Microbiol Lett: 2009, 291(2);151-6
[PubMed:19087206]
[WorldCat.org]
[DOI]
(I p)
Le Thi Tam, Christine Eymann, Dirk Albrecht, Rabea Sietmann, Frieder Schauer, Michael Hecker, Haike Antelmann
Differential gene expression in response to phenol and catechol reveals different metabolic activities for the degradation of aromatic compounds in Bacillus subtilis.
Environ Microbiol: 2006, 8(8);1408-27
[PubMed:16872404]
[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)
S Tobisch, J Stülke, M Hecker
Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site-directed mutagenesis.
J Bacteriol: 1999, 181(16);4995-5003
[PubMed:10438772]
[WorldCat.org]
[DOI]
(P p)
S Tobisch, P Glaser, S Krüger, M Hecker
Identification and characterization of a new beta-glucoside utilization system in Bacillus subtilis.
J Bacteriol: 1997, 179(2);496-506
[PubMed:8990303]
[WorldCat.org]
[DOI]
(P p)
