Difference between revisions of "KtrB"

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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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* '''Regulation:'''  
 
* '''Regulation:'''  
** induced if the energy charge is low ([[ydaO riboswitch]]) {{PubMed|23086297}}
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* '''Regulation:'''  
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
** expression is controlled via termination antitermination by the [[ydaO riboswitch]] {{PubMed|23086297,20511502}}  
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** expression is controlled via termination antitermination by the [[ydaO riboswitch]], expression is switched off upon binding od c-di-AMP {{PubMed|24141192,20511502}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''
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=Biological materials =
 
=Biological materials =
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=References=
 
=References=
  
<pubmed>12562800,20511502, 17932047 23086297 23598340 16990138 </pubmed>
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<pubmed>12562800,20511502, 17932047 23086297 23598340 16990138 24141192</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:08, 14 December 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
Sequences Protein DNA DNA_with_flanks
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:
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulation:
  • Regulatory mechanism:
    • expression is controlled via termination antitermination by the ydaO riboswitch, expression is switched off upon binding od c-di-AMP PubMed
  • Additional information:


Biological materials

  • 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

James W Nelson, Narasimhan Sudarsan, Kazuhiro Furukawa, Zasha Weinberg, Joy X Wang, Ronald R Breaker
Riboswitches in eubacteria sense the second messenger c-di-AMP.
Nat Chem Biol: 2013, 9(12);834-9
[PubMed:24141192] [WorldCat.org] [DOI] (I p)

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)

Ronald A Albright, José-Luís Vazquez Ibar, Chae Un Kim, Sol M Gruner, João Henrique Morais-Cabral
The RCK domain of the KtrAB K+ transporter: multiple conformations of an octameric ring.
Cell: 2006, 126(6);1147-59
[PubMed:16990138] [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)