Difference between revisions of "KinB"

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<pubmed>8576055,16166384,9299348,8497199,10094672,9426145,11069677,12618455,11902725,12618455,7592498, 21097618 19101565 23378509 23599347 </pubmed>
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<pubmed>8576055,16166384,9299348,8497199,10094672,9426145,11069677,12618455,11902725,12618455,7592498, 21097618 19101565 23378509 23599347 26152584</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:05, 13 July 2015

Gene name kinB
Synonyms
Essential no
Product two-component sensor kinase
Function initiation of sporulation
Gene expression levels in SubtiExpress: kinB
Interactions involving this protein in SubtInteract: KinB
Function and regulation of this protein in SubtiPathways:
kinB
MW, pI 47 kDa, 6.682
Gene length, protein length 1287 bp, 429 aa
Immediate neighbours patB, kapB
Sequences Protein DNA DNA_with_flanks
Genetic context
KinB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
KinB expression.png















Categories containing this gene/protein

protein modification, transcription factors and their control, phosphorelay, membrane proteins, phosphoproteins

This gene is a member of the following regulons

CodY regulon, stringent response

The gene

Basic information

  • Locus tag: BSU31450

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • autophosphorylation, phosphorylation of Spo0F
    • mainly active in the older, inner regions of a colony (with KinA) PubMed
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: six transmembrane segments, C-terminal histidine phosphotransferase domain
  • Modification: autophosphorylation on a His residue
  • Cofactor(s):
  • Effectors of protein activity:
    • activity is triggered at low respiratory activity, this depends on a functional interaction with the respiration apparatus PubMed

Database entries

  • Structure: 3D36 (from G. stearothermophilus, complex with Sda)
  • KEGG entry: [3]
  • 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

Your additional remarks

References

Roberto R Grau, Paula de Oña, Maritta Kunert, Cecilia Leñini, Ramses Gallegos-Monterrosa, Eisha Mhatre, Darío Vileta, Verónica Donato, Theresa Hölscher, Wilhelm Boland, Oscar P Kuipers, Ákos T Kovács
A Duo of Potassium-Responsive Histidine Kinases Govern the Multicellular Destiny of Bacillus subtilis.
mBio: 2015, 6(4);e00581
[PubMed:26152584] [WorldCat.org] [DOI] (I e)

Ilana Kolodkin-Gal, Alexander K W Elsholz, Christine Muth, Peter R Girguis, Roberto Kolter, Richard Losick
Respiration control of multicellularity in Bacillus subtilis by a complex of the cytochrome chain with a membrane-embedded histidine kinase.
Genes Dev: 2013, 27(8);887-99
[PubMed:23599347] [WorldCat.org] [DOI] (I p)

Shigeo Tojo, Kazutake Hirooka, Yasutaro Fujita
Expression of kinA and kinB of Bacillus subtilis, necessary for sporulation initiation, is under positive stringent transcription control.
J Bacteriol: 2013, 195(8);1656-65
[PubMed:23378509] [WorldCat.org] [DOI] (I p)

Anna L McLoon, Ilana Kolodkin-Gal, Shmuel M Rubinstein, Roberto Kolter, Richard Losick
Spatial regulation of histidine kinases governing biofilm formation in Bacillus subtilis.
J Bacteriol: 2011, 193(3);679-85
[PubMed:21097618] [WorldCat.org] [DOI] (I p)

Matthew J Bick, Valerie Lamour, Kanagalaghatta R Rajashankar, Yuliya Gordiyenko, Carol V Robinson, Seth A Darst
How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda.
J Mol Biol: 2009, 386(1);163-77
[PubMed:19101565] [WorldCat.org] [DOI] (I p)

Masaya Fujita, Richard Losick
Evidence that entry into sporulation in Bacillus subtilis is governed by a gradual increase in the level and activity of the master regulator Spo0A.
Genes Dev: 2005, 19(18);2236-44
[PubMed:16166384] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

M Jiang, W Shao, M Perego, J A Hoch
Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis.
Mol Microbiol: 2000, 38(3);535-42
[PubMed:11069677] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)

V Dartois, T Djavakhishvili, J A Hoch
KapB is a lipoprotein required for KinB signal transduction and activation of the phosphorelay to sporulation in Bacillus subtilis.
Mol Microbiol: 1997, 26(5);1097-108
[PubMed:9426145] [WorldCat.org] [DOI] (P p)

Y L Tzeng, J A Hoch
Molecular recognition in signal transduction: the interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis.
J Mol Biol: 1997, 272(2);200-12
[PubMed:9299348] [WorldCat.org] [DOI] (P p)

V Dartois, J Liu, J A Hoch
Alterations in the flow of one-carbon units affect KinB-dependent sporulation in Bacillus subtilis.
Mol Microbiol: 1997, 25(1);39-51
[PubMed:11902725] [WorldCat.org] [DOI] (P p)

V Dartois, T Djavakhishvili, J A Hoch
Identification of a membrane protein involved in activation of the KinB pathway to sporulation in Bacillus subtilis.
J Bacteriol: 1996, 178(4);1178-86
[PubMed:8576055] [WorldCat.org] [DOI] (P p)

M A Strauch
Delineation of AbrB-binding sites on the Bacillus subtilis spo0H, kinB, ftsAZ, and pbpE promoters and use of a derived homology to identify a previously unsuspected binding site in the bsuB1 methylase promote.
J Bacteriol: 1995, 177(23);6999-7002
[PubMed:7592498] [WorldCat.org] [DOI] (P p)

K A Trach, J A Hoch
Multisensory activation of the phosphorelay initiating sporulation in Bacillus subtilis: identification and sequence of the protein kinase of the alternate pathway.
Mol Microbiol: 1993, 8(1);69-79
[PubMed:8497199] [WorldCat.org] [DOI] (P p)