KipI

• Description: inhibitor of KinA, control of the phosphorelay
  
  

Gene name	kipI
Synonyms	ycsJ
Essential	no
Product	inhibitor of KinA
Function	control of the phosphorelay, initiation of sporulation
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

Categories containing this gene/protein

phosphorelay

This gene is a member of the following regulons

KipR regulon, TnrA regulon

The gene

Basic information

• Locus tag: BSU04080

Expression

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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: binding of KipA prevents KipI from binding to KinA PubMed

• Interactions: KipI-KinA PubMed, KipI-KipA PubMed

• Localization:

Database entries

• Structure: 2ZP2 PubMed

• UniProt: P60495

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ycsF-ycsG-ycsI-kipI-kipA-kipR-lipC PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:
  • KipR: transcription repression PubMed
  • TnrA: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)