Difference between revisions of "LicA"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU38570&redirect=T BSU38570] | ||
* '''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=BSU38570&redirect=T BSU38570] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3K1S 3K1S] (IIA(Cel) from ''B. anthracis'', 42% identity) | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3K1S 3K1S] (IIA(Cel) from ''B. anthracis'', 42% identity) |
Revision as of 15:09, 2 April 2014
- 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 |
Gene expression levels in SubtiExpress: licA | |
Interactions involving this protein in SubtInteract: LicA | |
Metabolic function and regulation of this protein in SubtiPathways: licA | |
MW, pI | 12 kDa, 4.641 |
Gene length, protein length | 330 bp, 110 aa |
Immediate neighbours | licH, licC |
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, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU38570
Phenotypes of a mutant
Database entries
- BsubCyc: BSU38570
- 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:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU38570
- 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:
- 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)