Difference between revisions of "KipI"
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|style="background:#ABCDEF;" align="center"|'''Function''' || control of the [[phosphorelay]], initiation of sporulation | |style="background:#ABCDEF;" align="center"|'''Function''' || control of the [[phosphorelay]], initiation of sporulation | ||
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| + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU04080 kipI] | ||
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/KipI KipI] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/KipI KipI] | ||
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|colspan="2" | '''Genetic context''' <br/> [[Image:kipI_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:kipI_context.gif]] | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
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| + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=kipI_459867_460589_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:kipI_expression.png|500px]] | ||
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* '''Operon:''' ''[[ycsF]]-[[ycsG]]-[[ycsI]]-[[kipI]]-[[kipA]]-[[kipR]]-[[lipC]]'' {{PubMed|9334321}} | * '''Operon:''' ''[[ycsF]]-[[ycsG]]-[[ycsI]]-[[kipI]]-[[kipA]]-[[kipR]]-[[lipC]]'' {{PubMed|9334321}} | ||
| − | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=kipI_459867_460589_1 kipI] {{PubMed|22383849}} |
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| + | * '''Sigma factor:''' | ||
* '''Regulation:''' | * '''Regulation:''' | ||
Revision as of 11:59, 7 August 2012
| Gene name | kipI |
| Synonyms | ycsJ |
| Essential | no |
| Product | inhibitor of KinA |
| Function | control of the phosphorelay, initiation of sporulation |
| Gene expression levels in SubtiExpress: kipI | |
| Interactions involving this protein in SubtInteract: KipI | |
| Function and regulation of this protein in SubtiPathways: Phosphorelay | |
| MW, pI | 26 kDa, 4.656 |
| Gene length, protein length | 720 bp, 240 aa |
| Immediate neighbours | ycsI, kipA |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU04080
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:
- Modification:
- Cofactor(s):
Database entries
- UniProt: P60495
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- 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
David A Jacques, David B Langley, Robert M G Hynson, Andrew E Whitten, Ann Kwan, J Mitchell Guss, Jill Trewhella
A novel structure of an antikinase and its inhibitor.
J Mol Biol: 2011, 405(1);214-26
[PubMed:21050859]
[WorldCat.org]
[DOI]
(I p)
Robert M G Hynson, Ann H Kwan, David A Jacques, Joel P Mackay, Jill Trewhella
1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis.
Biomol NMR Assign: 2010, 4(2);167-9
[PubMed:20524093]
[WorldCat.org]
[DOI]
(I p)
David A Jacques, David B Langley, Cy M Jeffries, Katherine A Cunningham, William F Burkholder, J Mitchell Guss, Jill Trewhella
Histidine kinase regulation by a cyclophilin-like inhibitor.
J Mol Biol: 2008, 384(2);422-35
[PubMed:18823995]
[WorldCat.org]
[DOI]
(I 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)
