KinA

• Description: two-component sensor kinase, phosphorylates Spo0F, part of the phosphorelay
  
  

Gene name	kinA
Synonyms	spoIIF, spoIIJ, gsiC, scoB, scoD
Essential	no
Product	two-component sensor kinase
Function	initiation of sporulation
Function and regulation of this protein in SubtiPathways: Phosphorelay
MW, pI	68 kDa, 5.491
Gene length, protein length	1818 bp, 606 aa
Immediate neighbours	pbpH, patA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU13990

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of Spo0F

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains: C-terminal histidine phosphotransferase domain

• Modification: autophosphorylation on a His residue

• Cofactor(s):

• Effectors of protein activity: interaction with KipI or Sda inhibits autophosphorylation of KinA PubMed

• Interactions: KinA-KipI PubMed, KinA-Sda PubMed, Spo0F-KinA

• Localization:

Database entries

• Structure: 2VLG (PAS domain)

• UniProt: P16497

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: kinA PubMed

• Sigma factor: SigH PubMed

• Regulation:
  • expressed under conditions that trigger sporulation (Spo0A) PubMed

• Regulatory mechanism:
  • Spo0A: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Prahathees Eswaramoorthy, Masaya Fujita
Systematic domain deletion analysis of the major sporulation kinase in Bacillus subtilis.
J Bacteriol: 2010, 192(6);1744-8
[PubMed:20081035] [WorldCat.org] [DOI] (I p)

Prahathees Eswaramoorthy, Tao Guo, Masaya Fujita
In vivo domain-based functional analysis of the major sporulation sensor kinase, KinA, in Bacillus subtilis.
J Bacteriol: 2009, 191(17);5358-68
[PubMed:19561131] [WorldCat.org] [DOI] (I p)

Kazuo Kobayashi, Ritsuko Kuwana, Hiromu Takamatsu
kinA mRNA is missing a stop codon in the undomesticated Bacillus subtilis strain ATCC 6051.
Microbiology (Reading): 2008, 154(Pt 1);54-63
[PubMed:18174125] [WorldCat.org] [DOI] (P p)

Andrew E Whitten, David A Jacques, Boualem Hammouda, Tracey Hanley, Glenn F King, J Mitchell Guss, Jill Trewhella, David B Langley
The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition.
J Mol Biol: 2007, 368(2);407-20
[PubMed:17350039] [WorldCat.org] [DOI] (P 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)

Susan L Rowland, William F Burkholder, Katherine A Cunningham, Mark W Maciejewski, Alan D Grossman, Glenn F King
Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis.
Mol Cell: 2004, 13(5);689-701
[PubMed:15023339] [WorldCat.org] [DOI] (P p)

Sophie J Stephenson, Marta Perego
Interaction surface of the Spo0A response regulator with the Spo0E phosphatase.
Mol Microbiol: 2002, 44(6);1455-67
[PubMed:12067336] [WorldCat.org] [DOI] (P p)

K Stephenson, J A Hoch
PAS-A domain of phosphorelay sensor kinase A: a catalytic ATP-binding domain involved in the initiation of development in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2001, 98(26);15251-6
[PubMed:11734624] [WorldCat.org] [DOI] (P p)

L Wang, C Fabret, K Kanamaru, K Stephenson, V Dartois, M Perego, J A Hoch
Dissection of the functional and structural domains of phosphorelay histidine kinase A of Bacillus subtilis.
J Bacteriol: 2001, 183(9);2795-802
[PubMed:11292798] [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)

M Fujita, Y Sadaie
Feedback loops involving Spo0A and AbrB in in vitro transcription of the genes involved in the initiation of sporulation in Bacillus subtilis.
J Biochem: 1998, 124(1);98-104
[PubMed:9644251] [WorldCat.org] [DOI] (P p)

C E Grimshaw, S Huang, C G Hanstein, M A Strauch, D Burbulys, L Wang, J A Hoch, J M Whiteley
Synergistic kinetic interactions between components of the phosphorelay controlling sporulation in Bacillus subtilis.
Biochemistry: 1998, 37(5);1365-75
[PubMed:9477965] [WorldCat.org] [DOI] (P p)

L Wang, R Grau, M Perego, J A Hoch
A novel histidine kinase inhibitor regulating development in Bacillus subtilis.
Genes Dev: 1997, 11(19);2569-79
[PubMed:9334321] [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)

M Predich, G Nair, I Smith
Bacillus subtilis early sporulation genes kinA, spo0F, and spo0A are transcribed by the RNA polymerase containing sigma H.
J Bacteriol: 1992, 174(9);2771-8
[PubMed:1569009] [WorldCat.org] [DOI] (P p)

D Burbulys, K A Trach, J A Hoch
Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay.
Cell: 1991, 64(3);545-52
[PubMed:1846779] [WorldCat.org] [DOI] (P p)

M Perego, S P Cole, D Burbulys, K Trach, J A Hoch
Characterization of the gene for a protein kinase which phosphorylates the sporulation-regulatory proteins Spo0A and Spo0F of Bacillus subtilis.
J Bacteriol: 1989, 171(11);6187-96
[PubMed:2509430] [WorldCat.org] [DOI] (P p)