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
Gene expression levels in SubtiExpress: kinA
Interactions involving this protein in SubtInteract: KinA
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
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, phosphoproteins

This gene is a member of the following regulons

SigH regulon, Spo0A regulon, stringent response

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
  • mainly active in the older, inner regions of a colony (with KinB) PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:
  • three tandem PAS domains in the N-terminal region of KinA, the second PAS domain is the major N-terminal determinant of KinA dimerization PubMed
  • the first PAS domain is required for NAD(+) binding PubMed
  • 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
  • autophosphorylation is inhibited by SivA and BslA PubMed
  • activated by interaction with NAD(+) that indicated poor respiratory activity of the cell PubMed

• Interactions:
  • forms tetramers PubMed
  • KinA-KipI PubMed
  • KinA-Sda PubMed
  • Spo0F-KinA

• Localization:
  • cytoplasm

Database entries

• Structure: 2VLG (PAS domain)

• UniProt: P16497

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: kinA PubMed

• Expression browser: kinA PubMed

• Sigma factor: SigH PubMed

• Regulation:
  • expressed under conditions that trigger sporulation (Spo0A) PubMed
  • induced upon addition of decoyinine (positive stringent response) PubMed

• Regulatory mechanism:
  • Spo0A: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Liza Gross
Built-in timer delays differentiation.
PLoS Biol: 2012, 10(1);e1001254
[PubMed:22303284] [WorldCat.org] [DOI] (I p)

Original Publications

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)

Brit Winnen, Eric Anderson, James L Cole, Glenn F King, Susan L Rowland
Role of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA.
J Bacteriol: 2013, 195(10);2349-58
[PubMed:23504013] [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)

Sharon Garti-Levi, Ashlee Eswara, Yoav Smith, Masaya Fujita, Sigal Ben-Yehuda
Novel modulators controlling entry into sporulation in Bacillus subtilis.
J Bacteriol: 2013, 195(7);1475-83
[PubMed:23335417] [WorldCat.org] [DOI] (I p)

Jatin Narula, Seram N Devi, Masaya Fujita, Oleg A Igoshin
Ultrasensitivity of the Bacillus subtilis sporulation decision.
Proc Natl Acad Sci U S A: 2012, 109(50);E3513-22
[PubMed:23169620] [WorldCat.org] [DOI] (I p)

Angel E Dago, Alexander Schug, Andrea Procaccini, James A Hoch, Martin Weigt, Hendrik Szurmant
Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis.
Proc Natl Acad Sci U S A: 2012, 109(26);E1733-42
[PubMed:22670053] [WorldCat.org] [DOI] (I p)

Joe H Levine, Michelle E Fontes, Jonathan Dworkin, Michael B Elowitz
Pulsed feedback defers cellular differentiation.
PLoS Biol: 2012, 10(1);e1001252
[PubMed:22303282] [WorldCat.org] [DOI] (I p)

Prahathees Eswaramoorthy, Ashlee Dravis, Seram Nganbiton Devi, Monika Vishnoi, Hoang-Anh Dao, Masaya Fujita
Expression level of a chimeric kinase governs entry into sporulation in Bacillus subtilis.
J Bacteriol: 2011, 193(22);6113-22
[PubMed:21926229] [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)

Prahathees Eswaramoorthy, Daniel Duan, Jeffrey Dinh, Ashlee Dravis, Seram Nganbiton Devi, Masaya Fujita
The threshold level of the sensor histidine kinase KinA governs entry into sporulation in Bacillus subtilis.
J Bacteriol: 2010, 192(15);3870-82
[PubMed:20511506] [WorldCat.org] [DOI] (I p)

Prahathees Eswaramoorthy, Jeffrey Dinh, Daniel Duan, Oleg A Igoshin, Masaya Fujita
Single-cell measurement of the levels and distributions of the phosphorelay components in a population of sporulating Bacillus subtilis cells.
Microbiology (Reading): 2010, 156(Pt 8);2294-2304
[PubMed:20413551] [WorldCat.org] [DOI] (I p)

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)