Difference between revisions of "KtrB"

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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
 
** KtrB forms dimers {{PubMed|17932047}}  
 
** KtrB forms dimers {{PubMed|17932047}}  
** [[KtrA]]-[[KtrB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/12562800 PubMed]
+
** [[KtrA]]-[[KtrB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/12562800 PubMed], composed of an octameric [[KtrA]] ring and two [[KtrB]] dimers {{PubMed|23598340}}
  
 
* '''[[Localization]]:''' integral membrane protein [http://www.ncbi.nlm.nih.gov/sites/entrez/12562800 PubMed]
 
* '''[[Localization]]:''' integral membrane protein [http://www.ncbi.nlm.nih.gov/sites/entrez/12562800 PubMed]
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* '''Structure:'''
 
* '''Structure:'''
 +
** [http://www.pdb.org/pdb/explore/explore.do?structureId=4J7C 4J7C] (the [[KtrA]]-[[KtrB]] complex) {{PubMed|23598340}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O32081 O32081]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O32081 O32081]
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ktrB_3189089_3190426_1 ktrB] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ktrB_3189089_3190426_1 ktrB] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
+
* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
  
<pubmed>12562800,20511502, 17932047 23086297</pubmed>
+
<pubmed>12562800,20511502, 17932047 23086297 23598340 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:06, 22 April 2013

  • Description: high affinity potassium transporter KtrA-KtrB, integral membrane subunit

Gene name ktrB
Synonyms yubG
Essential no
Product high affinity potassium transporter KtrA-KtrB,
integral membrane subunit (proton symport)
Function potassium uptake
Gene expression levels in SubtiExpress: ktrB
Interactions involving this protein in SubtInteract: KtrB
Metabolic function and regulation of this protein in SubtiPathways:
Metal ion homeostasis, Stress
MW, pI 48 kDa, 10.116
Gene length, protein length 1335 bp, 445 aa
Immediate neighbours ktrA, yubF
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YubG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
KtrB expression.png















Categories containing this gene/protein

transporters/ other, metal ion homeostasis (K, Na, Ca, Mg), coping with hyper-osmotic stress, membrane proteins

This gene is a member of the following regulons

YdaO riboswitch

The gene

Basic information

  • Locus tag: BSU31100

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): KtrD

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and 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

Ricardo S Vieira-Pires, Andras Szollosi, João H Morais-Cabral
The structure of the KtrAB potassium transporter.
Nature: 2013, 496(7445);323-8
[PubMed:23598340] [WorldCat.org] [DOI] (I p)

Peter Y Watson, Martha J Fedor
The ydaO motif is an ATP-sensing riboswitch in Bacillus subtilis.
Nat Chem Biol: 2012, 8(12);963-5
[PubMed:23086297] [WorldCat.org] [DOI] (I p)

Kirsten F Block, Ming C Hammond, Ronald R Breaker
Evidence for widespread gene control function by the ydaO riboswitch candidate.
J Bacteriol: 2010, 192(15);3983-9
[PubMed:20511502] [WorldCat.org] [DOI] (I p)

Ronald A Albright, Kyu Joh, João H Morais-Cabral
Probing the structure of the dimeric KtrB membrane protein.
J Biol Chem: 2007, 282(48);35046-55
[PubMed:17932047] [WorldCat.org] [DOI] (P p)

Gudrun Holtmann, Evert P Bakker, Nobuyuki Uozumi, Erhard Bremer
KtrAB and KtrCD: two K+ uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity.
J Bacteriol: 2003, 185(4);1289-98
[PubMed:12562800] [WorldCat.org] [DOI] (P p)