Difference between revisions of "KipA"
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<br/><br/><br/><br/><br/><br/> | <br/><br/><br/><br/><br/><br/> | ||
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+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[phosphorelay]]}} | ||
+ | |||
+ | = This gene is a member of the following [[regulons]] = | ||
+ | {{SubtiWiki regulon|[[KipR regulon]]}}, | ||
+ | {{SubtiWiki regulon|[[TnrA regulon]]}} | ||
=The gene= | =The gene= | ||
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− | + | ||
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=The protein= | =The protein= | ||
Revision as of 16:49, 8 December 2010
- Description: antagonist of KipI, control of the phosphorelay
Gene name | kipA |
Synonyms | |
Essential | no |
Product | antagonist of KipI |
Function | control of the phosphorelay, initiation of sporulation |
Function and regulation of this protein in SubtiPathways: Phosphorelay | |
MW, pI | 36 kDa, 5.465 |
Gene length, protein length | 1011 bp, 337 aa |
Immediate neighbours | kipI, kipR |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU04090
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):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- UniProt: Q7WY77
- 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
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)
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)