Difference between revisions of "OpuAA"

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= Categories containing this gene/protein =
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{{SubtiWiki category|[[ABC transporters]]}},
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{{SubtiWiki category|[[coping with hyper-osmotic stress]]}},
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{{SubtiWiki category|[[membrane proteins]]}}
 
=The protein=
 
=The protein=
  

Revision as of 18:33, 30 November 2010

Gene name opuAA
Synonyms
Essential no
Product glycine betaine ABC transporter (ATP-binding protein)
Function compatible solute transport
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 46 kDa, 5.107
Gene length, protein length 1254 bp, 418 aa
Immediate neighbours yceK, opuAB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
OpuAA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU02980

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

Categories containing this gene/protein

ABC transporters, coping with hyper-osmotic stress, membrane proteins

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + H2O + quaternary amine(Out) = ADP + phosphate + quaternary amine(In) (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: associated to the membrane (via OpuAB) PubMed

Database entries

  • Structure:
  • KEGG entry: [2]

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

Carsten Horn, Stefan Jenewein, Britta Tschapek, Werner Bouschen, Sabine Metzger, Erhard Bremer, Lutz Schmitt
Monitoring conformational changes during the catalytic cycle of OpuAA, the ATPase subunit of the ABC transporter OpuA from Bacillus subtilis.
Biochem J: 2008, 412(2);233-44
[PubMed:18321243] [WorldCat.org] [DOI] (I p)

Carsten Horn, Stefan Jenewein, Linda Sohn-Bösser, Erhard Bremer, Lutz Schmitt
Biochemical and structural analysis of the Bacillus subtilis ABC transporter OpuA and its isolated subunits.
J Mol Microbiol Biotechnol: 2005, 10(2-4);76-91
[PubMed:16645306] [WorldCat.org] [DOI] (P p)

Carsten Horn, Erhard Bremer, Lutz Schmitt
Functional overexpression and in vitro re-association of OpuA, an osmotically regulated ABC-transport complex from Bacillus subtilis.
FEBS Lett: 2005, 579(25);5765-8
[PubMed:16225868] [WorldCat.org] [DOI] (P p)

Carsten Horn, Erhard Bremer, Lutz Schmitt
Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis.
J Mol Biol: 2003, 334(3);403-19
[PubMed:14623183] [WorldCat.org] [DOI] (P p)

Y Quentin, G Fichant, F Denizot
Inventory, assembly and analysis of Bacillus subtilis ABC transport systems.
J Mol Biol: 1999, 287(3);467-84
[PubMed:10092453] [WorldCat.org] [DOI] (P p)

B Kempf, E Bremer
OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis.
J Biol Chem: 1995, 270(28);16701-13
[PubMed:7622480] [WorldCat.org] [DOI] (P p)