Difference between revisions of "SepF"

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* '''Description:''' part of the divisome, recruits [[FtsZ]] to the membrane <br/><br/>
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* '''Description:''' part of the [[divisome]], recruits [[FtsZ]] to the membrane <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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* less efficient cell division results in longer cells. Electron microscopy reveals strongly distorted division septa.
 
* less efficient cell division results in longer cells. Electron microscopy reveals strongly distorted division septa.
 
* the ''[[sepF]]'' mutation in combination with a constitutively active form of [[WalR]] ([[WalR]]-R204C) results in the formation of cell wall-less L-forms {{PubMed|22122227}}
 
* the ''[[sepF]]'' mutation in combination with a constitutively active form of [[WalR]] ([[WalR]]-R204C) results in the formation of cell wall-less L-forms {{PubMed|22122227}}
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* the ''sepF'' mutation is synthetically lethal in combination with an ''[[ezrA]]'' mutation or an ''[[ftsA]]'' mutation
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* the ''sepF'' mutation is synthetically lethal in combination with an ''[[ezrA]]'' mutation or an ''[[ftsA]]'' mutation {{PubMed|24218584}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Catalyzed reaction/ biological activity:'''  
 
* '''Catalyzed reaction/ biological activity:'''  
 
** SepF assembles into very large (∼50 nm diameter) rings. These rings are able to bundle [[FtsZ]] protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules {{PubMed|21224850}}
 
** SepF assembles into very large (∼50 nm diameter) rings. These rings are able to bundle [[FtsZ]] protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules {{PubMed|21224850}}
 +
** SepF anchors [[FtsZ]] bundles to the membrane {{PubMed|24218584}}
  
 
* '''Protein family:''' sepF family (according to Swiss-Prot)
 
* '''Protein family:''' sepF family (according to Swiss-Prot)
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
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* '''Domains:'''  
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* '''[[Domains]]:'''  
 
** N-terminal amphipatic helix for membrane binding {{PubMed|24218584}}
 
** N-terminal amphipatic helix for membrane binding {{PubMed|24218584}}
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** C-terminal [[FtsZ]]-binding domain {{PubMed|24218584}}
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** C-terminal globular [[FtsZ]]-binding domain {{PubMed|24218584}}
  
 
* '''Modification:'''
 
* '''Modification:'''
  
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* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
 
* '''[[SubtInteract|Interactions]]:'''  
 
* '''[[SubtInteract|Interactions]]:'''  
 +
** forms filaments that are made up of dimers {{PubMed|24218584}}
 
** [[FtsZ]] (extreme C terminus of [[FtsZ]])-[[SepF]] {{PubMed|24218584,22912848,16420366}}
 
** [[FtsZ]] (extreme C terminus of [[FtsZ]])-[[SepF]] {{PubMed|24218584,22912848,16420366}}
 
   
 
   

Revision as of 10:33, 15 December 2013

  • Description: part of the divisome, recruits FtsZ to the membrane

Gene name sepF
Synonyms ylmF
Essential no
Product FtsZ-interacting protein
Function recruitment of FtsZ
Gene expression levels in SubtiExpress: sepF
Interactions involving this protein in SubtInteract: SepF
MW, pI 17 kDa, 4.863
Gene length, protein length 447 bp, 149 aa
Immediate neighbours ylmE, ylmG
Sequences Protein DNA DNA_with_flanks
Genetic context
YlmF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SepF expression.png















Categories containing this gene/protein

cell division, membrane proteins

This gene is a member of the following regulons

Spo0A regulon

The gene

Basic information

  • Locus tag: BSU15390

Phenotypes of a mutant

  • perturbation of the formation of properly formed division septa
  • less efficient cell division results in longer cells. Electron microscopy reveals strongly distorted division septa.
  • the sepF mutation in combination with a constitutively active form of WalR (WalR-R204C) results in the formation of cell wall-less L-forms PubMed
  • the sepF mutation is synthetically lethal in combination with an ezrA mutation or an ftsA mutation PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • SepF assembles into very large (∼50 nm diameter) rings. These rings are able to bundle FtsZ protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules PubMed
    • SepF anchors FtsZ bundles to the membrane PubMed
  • Protein family: sepF family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Leendert Hamoen, CBCB, Newcastle University, UK

Shu Ishikawa, Nara Institute of Science and Technology, Nara, Japan

Your additional remarks

SepF mutation is synthetic lethal in combination with an ezrA mutation or an ftsA mutation.

References

Reviews


Original Publications

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