Difference between revisions of "OpuAB"
| Line 75: | Line 75: | ||
* '''Interactions:''' | * '''Interactions:''' | ||
| − | * '''Localization:''' | + | * '''Localization:''' membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] |
=== Database entries === | === Database entries === | ||
| Line 121: | Line 121: | ||
=References= | =References= | ||
| + | # Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing ''Bacillus subtilis'' by divergent approaches. Proteomics '''8:''' 4123-4136 [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | ||
# Kempf B, Bremer E. (1995) OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. ''J Biol Chem.'' '''Jul 14;270(28):''' 16701-13. [http://www.ncbi.nlm.nih.gov/sites/entrez/7622480 PubMed] | # Kempf B, Bremer E. (1995) OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. ''J Biol Chem.'' '''Jul 14;270(28):''' 16701-13. [http://www.ncbi.nlm.nih.gov/sites/entrez/7622480 PubMed] | ||
# Horn C, Bremer E, Schmitt L. (2005) Functional overexpression and in vitro re-association of OpuA, an osmotically regulated ABC-transport complex from Bacillus subtilis. ''FEBS Lett.'' '''Oct 24;579(25):''' 5765-8. [http://www.ncbi.nlm.nih.gov/sites/entrez/16225868 PubMed] | # Horn C, Bremer E, Schmitt L. (2005) Functional overexpression and in vitro re-association of OpuA, an osmotically regulated ABC-transport complex from Bacillus subtilis. ''FEBS Lett.'' '''Oct 24;579(25):''' 5765-8. [http://www.ncbi.nlm.nih.gov/sites/entrez/16225868 PubMed] | ||
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | ||
Revision as of 14:47, 25 March 2009
- Description: glycine betaine ABC transporter (permease)
| Gene name | opuAB |
| Synonyms | |
| Essential | no |
| Product | glycine betaine ABC transporter (permease) |
| Function | compatible solute transport |
| MW, pI | 30 kDa, 9.837 |
| Gene length, protein length | 846 bp, 282 aa |
| Immediate neighbours | opuAA, opuAC |
| Gene sequence (+200bp) | Protein sequence |
| Caution: The sequence for this gene in SubtiList contains errors | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Coordinates:
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 family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: membrane associated PubMed
Database entries
- Structure:
- Swiss prot entry:
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
- Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
- Kempf B, Bremer E. (1995) OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. J Biol Chem. Jul 14;270(28): 16701-13. PubMed
- Horn C, Bremer E, Schmitt L. (2005) Functional overexpression and in vitro re-association of OpuA, an osmotically regulated ABC-transport complex from Bacillus subtilis. FEBS Lett. Oct 24;579(25): 5765-8. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
