OpuBC

• Description: choline ABC transporter (binding protein)
  
  

Gene name	opuBC
Synonyms	proX
Essential	no
Product	choline ABC transporter (binding protein)
Function	compatible solute transport
Gene expression levels in SubtiExpress: opuBC
Interactions involving this protein in SubtInteract: OpuBC
Metabolic function and regulation of this protein in SubtiPathways: opuBC
MW, pI	34 kDa, 6.618
Gene length, protein length	918 bp, 306 aa
Immediate neighbours	opuBD, opuBB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

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

This gene is a member of the following regulons

GbsR regulon, OpcR regulon

The gene

Basic information

• Locus tag: BSU33710

Database entries

• BsubCyc: BSU33710

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): OpuCC

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • OpuBA-(OpuBB-OpuBD)-OpuBC PubMed

• Localization:
  • associated to the membrane (via OpuBB-OpuBD) PubMed
  • lipoprotein PubMed

Database entries

• BsubCyc: BSU33710

• Structure: 3R6U

• UniProt: Q45462

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: opuBA-opuBB-opuBC-opuBD PubMed

• Expression browser: opuBC PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by salt stress PubMed
  • induced by choline (GbsR) PubMed

• Regulatory mechanism:
  • GbsR: transcription repression PubMed
  • OpcR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Chun-Hao Lee, Tien-Yu Wu, Gwo-Chyuan Shaw
Involvement of OpcR, a GbsR-type transcriptional regulator, in negative regulation of two evolutionarily closely related choline uptake genes in Bacillus subtilis.
Microbiology (Reading): 2013, 159(Pt 10);2087-2096
[PubMed:23960087] [WorldCat.org] [DOI] (I p)

Gabriele Nau-Wagner, Daniela Opper, Anne Rolbetzki, Jens Boch, Bettina Kempf, Tamara Hoffmann, Erhard Bremer
Genetic control of osmoadaptive glycine betaine synthesis in Bacillus subtilis through the choline-sensing and glycine betaine-responsive GbsR repressor.
J Bacteriol: 2012, 194(10);2703-14
[PubMed:22408163] [WorldCat.org] [DOI] (I p)

Marco Pittelkow, Britta Tschapek, Sander H J Smits, Lutz Schmitt, Erhard Bremer
The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline.
J Mol Biol: 2011, 411(1);53-67
[PubMed:21658392] [WorldCat.org] [DOI] (I p)

Yang Du, Wei-Wei Shi, Yong-Xing He, Yi-Hu Yang, Cong-Zhao Zhou, Yuxing Chen
Structures of the substrate-binding protein provide insights into the multiple compatible solute binding specificities of the Bacillus subtilis ABC transporter OpuC.
Biochem J: 2011, 436(2);283-9
[PubMed:21366542] [WorldCat.org] [DOI] (I p)

Tamara Hoffmann, Erhard Bremer
Protection of Bacillus subtilis against cold stress via compatible-solute acquisition.
J Bacteriol: 2011, 193(7);1552-62
[PubMed:21296969] [WorldCat.org] [DOI] (I p)

R M Kappes, B Kempf, S Kneip, J Boch, J Gade, J Meier-Wagner, E Bremer
Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis.
Mol Microbiol: 1999, 32(1);203-16
[PubMed:10216873] [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)

G Nau-Wagner, J Boch, Le Good JA, E Bremer
High-affinity transport of choline-O-sulfate and its use as a compatible solute in Bacillus subtilis.
Appl Environ Microbiol: 1999, 65(2);560-8
[PubMed:9925583] [WorldCat.org] [DOI] (P p)