Difference between revisions of "OpuAB"
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=References= | =References= | ||
+ | <pubmed>18763711 7622480 16225868, </pubmed> | ||
# 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] | # 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 19:19, 8 June 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 |
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: BSU02990
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: ABC transmembrane type-1 domain (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), membrane associated PubMed
Database entries
- Structure:
- Swiss prot entry: P46921
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Erhard Bremer, University of Marburg, Germany homepage
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