Difference between revisions of "KinB"
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=== Additional information=== | === Additional information=== | ||
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| − | |||
| − | |||
=The protein= | =The protein= | ||
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=3D36 3D36] (from G. stearothermophilus, complex with Sda) | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=3D36 3D36] (from G. stearothermophilus, complex with [[Sda]]) |
* '''UniProt:''' [http://www.uniprot.org/uniprot/Q08430 Q08430] | * '''UniProt:''' [http://www.uniprot.org/uniprot/Q08430 Q08430] | ||
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=References= | =References= | ||
| − | <pubmed>8576055,16166384,9299348,8497199,10094672,9426145,11069677,12618455,11902725,12618455,7592498, 21097618 </pubmed> | + | <pubmed>8576055,16166384,9299348,8497199,10094672,9426145,11069677,12618455,11902725,12618455,7592498, 21097618 19101565 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 13:36, 27 December 2010
- Description: two-component sensor kinase, phosphorylates Spo0F, part of the phosphorelay
| Gene name | kinB |
| Synonyms | |
| Essential | no |
| Product | two-component sensor kinase |
| Function | initiation of sporulation |
| Function and regulation of this protein in SubtiPathways: Phosphorelay | |
| MW, pI | 47 kDa, 6.682 |
| Gene length, protein length | 1287 bp, 429 aa |
| Immediate neighbours | patB, kapB |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
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
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:
- 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:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- UniProt: Q08430
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- 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
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)
