KtrA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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]

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

• Interactions:
  • KtrA-KtrB PubMed, composed of an octameric KtrA ring and two KtrB dimers PubMed

• Localization: peripheral membrane protein PubMed

Database entries

• Structure:
  • 1LSU (complex with NADH)
  • 2HMW ( complex with ATP)
  • 4J7C (the KtrA-KtrB complex) PubMed

• UniProt: O32080

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: ktrA-ktrB PubMed

• Expression browser: ktrA PubMed

• Sigma factor:

• Regulation:
  • induced if the energy charge is low (ydaO riboswitch) PubMed

• Regulatory mechanism:
  • expression is controlled via termination antitermination by the ydaO riboswitch PubMed

• Additional information:

Biological materials

• Mutant:
  • 1A954 ( ktrA::kan), PubMed, available at BGSC
  • GHB1 (D(ktrA-ktrB)::aphA3), available in Erhard Bremer's lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Erhard Bremer, University of Marburg, Germany homepage

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)