KinB

• Description: two-component sensor kinase, phosphorylates Spo0F, part of the phosphorelay, senses changes in respiratory activity
  
  

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

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

Database entries

• BsubCyc: BSU31450

• DBTBS entry: [1]

• SubtiList entry: [2]

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
  • sensing potassium level in the medium during initiation of sliding sliding PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:
  • six transmembrane segments, C-terminal histidine phosphotransferase domain
  • selectivity filter sequence of potassium channels that is required for sliding but not for sporulation PubMed

• 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

• Interactions:
  • KinB-Sda
  • KinB-Spo0F
  • KinB-CtaC PubMed
  • KinB-QcrC PubMed

• Localization: cell membrane (integral membrane protein) PubMed

Database entries

• BsubCyc: BSU31450

• Structure: 3D36 (from G. stearothermophilus, complex with Sda)

• UniProt: Q08430

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: kinB-kapB PubMed

• Expression browser: kinB PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • induced upon addition of decoyinine (positive stringent response) PubMed

• Regulatory mechanism:
  • CodY: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:
  • JH19980 (kinB::tet) PubMed

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)