Difference between revisions of "KtrA"

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(Phenotypes of a mutant)
(Phenotypes of a mutant)
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
KtrAB mutant of 3610 is reduced in sliding (dendritic spreading)
+
KtrAB mutant of 3610 is reduced in sliding (dendritic spreading) <pubmed> 16321950 </pubmed>
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 07:10, 19 July 2013

  • Description: high affinity potassium transporter KtrA-KtrB, peripheric membrane component (proton symport)

Gene name ktrA
Synonyms yuaA
Essential no
Product high affinity potassium transporter KtrA-KtrB,
peripheric membrane component (proton symport)
Function potassium uptake
Gene expression levels in SubtiExpress: ktrA
Interactions involving this protein in SubtInteract: KtrA
Metabolic function and regulation of this protein in SubtiPathways:
Metal ion homeostasis, Stress
MW, pI 24 kDa, 5.981
Gene length, protein length 666 bp, 222 aa
Immediate neighbours bslA, ktrB
Sequences Protein DNA DNA_with_flanks
Genetic context
YuaA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
KtrA 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: BSU31090

Phenotypes of a mutant

KtrAB mutant of 3610 is reduced in sliding (dendritic spreading)

Rebecca F Kinsinger, Daniel B Kearns, Marina Hale, Ray Fall
Genetic requirements for potassium ion-dependent colony spreading in Bacillus subtilis.
J Bacteriol: 2005, 187(24);8462-9
[PubMed:16321950] [WorldCat.org] [DOI] (P p)


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): KtrC

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
    • the protein binds c-di-AMP PubMed

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • 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

Rebecca M Corrigan, Ivan Campeotto, Tharshika Jeganathan, Kevin G Roelofs, Vincent T Lee, Angelika Gründling
Systematic identification of conserved bacterial c-di-AMP receptor proteins.
Proc Natl Acad Sci U S A: 2013, 110(22);9084-9
[PubMed:23671116] [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, 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)

Jeffrey E Barrick, Keith A Corbino, Wade C Winkler, Ali Nahvi, Maumita Mandal, Jennifer Collins, Mark Lee, Adam Roth, Narasimhan Sudarsan, Inbal Jona, J Kenneth Wickiser, Ronald R Breaker
New RNA motifs suggest an expanded scope for riboswitches in bacterial genetic control.
Proc Natl Acad Sci U S A: 2004, 101(17);6421-6
[PubMed:15096624] [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)