Difference between revisions of "ScpA"

From SubtiWiki
Jump to: navigation, search
Line 37: Line 37:
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
 
 
 
<br/><br/>
 
<br/><br/>
  
Line 95: Line 91:
 
* '''[[SubtInteract|Interactions]]:'''  
 
* '''[[SubtInteract|Interactions]]:'''  
 
** present as stable monomer {{PubMed|22385855}}
 
** present as stable monomer {{PubMed|22385855}}
** [[ScpA]]-[[Smc]] {{PubMed|22385855,12100548}}
+
** [[ScpA]]-[[Smc]] {{PubMed|23353789,22385855,12100548}}
 
** [[ScpA]]-[[ScpB]] {{PubMed|12100548}}  
 
** [[ScpA]]-[[ScpB]] {{PubMed|12100548}}  
  
Line 103: Line 99:
  
 
* '''Structure:'''
 
* '''Structure:'''
 +
** [http://www.pdb.org/pdb/explore/explore.do?structureId=3ZGX 3ZGX] (complex between the head domain of [[Smc]] (aa 1 - 219 and 983 - 1186) and the N-terminal winged-helix domain of [[ScpA]]) {{PubMed|23353789}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P35154 P35154]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P35154 P35154]
Line 118: Line 115:
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=scpA_2425831_2426586_-1 scpA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=scpA_2425831_2426586_-1 scpA] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
+
* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
Line 146: Line 143:
  
 
=References=
 
=References=
<pubmed>22385855</pubmed>
+
<pubmed>22385855 23353789 </pubmed>
 
<pubmed>12100548,12421306,12065423,7934830, 16479537, 19450516 15009890 11948165</pubmed>
 
<pubmed>12100548,12421306,12065423,7934830, 16479537, 19450516 15009890 11948165</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:40, 1 February 2013

  • Description: DNA segregation and condensation protein

Gene name scpA
Synonyms ypuG
Essential yes PubMed
Product DNA segregation and condensation protein
Function maintenance of chromosome structure
Gene expression levels in SubtiExpress: scpA
Interactions involving this protein in SubtInteract: ScpA
MW, pI 29 kDa, 4.788
Gene length, protein length 753 bp, 251 aa
Immediate neighbours scpB, ypuF
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YpuG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ScpA expression.png















Categories containing this gene/protein

DNA condensation/ segregation, essential genes

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU23220

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: scpA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
    • 3ZGX (complex between the head domain of Smc (aa 1 - 219 and 983 - 1186) and the N-terminal winged-helix domain of ScpA) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • 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

Frank Bürmann, Ho-Chul Shin, Jérôme Basquin, Young-Min Soh, Victor Giménez-Oya, Yeon-Gil Kim, Byung-Ha Oh, Stephan Gruber
An asymmetric SMC-kleisin bridge in prokaryotic condensin.
Nat Struct Mol Biol: 2013, 20(3);371-9
[PubMed:23353789] [WorldCat.org] [DOI] (I p)

M E Fuentes-Perez, E J Gwynn, M S Dillingham, F Moreno-Herrero
Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.
Biophys J: 2012, 102(4);839-48
[PubMed:22385855] [WorldCat.org] [DOI] (I p)

Stephan Gruber, Jeff Errington
Recruitment of condensin to replication origin regions by ParB/SpoOJ promotes chromosome segregation in B. subtilis.
Cell: 2009, 137(4);685-96
[PubMed:19450516] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Etienne Dervyn, Marie-Françoise Noirot-Gros, Peggy Mervelet, Steven McGovern, S Dusko Ehrlich, Patrice Polard, Philippe Noirot
The bacterial condensin/cohesin-like protein complex acts in DNA repair and regulation of gene expression.
Mol Microbiol: 2004, 51(6);1629-40
[PubMed:15009890] [WorldCat.org] [DOI] (P p)

Janet C Lindow, Masayoshi Kuwano, Shigeki Moriya, Alan D Grossman
Subcellular localization of the Bacillus subtilis structural maintenance of chromosomes (SMC) protein.
Mol Microbiol: 2002, 46(4);997-1009
[PubMed:12421306] [WorldCat.org] [DOI] (P p)

Jörg Soppa, Kazuo Kobayashi, Marie-Françoise Noirot-Gros, Dieter Oesterhelt, S Dusko Ehrlich, Etienne Dervyn, Naotake Ogasawara, Shigeki Moriya
Discovery of two novel families of proteins that are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members ScpA and ScpB.
Mol Microbiol: 2002, 45(1);59-71
[PubMed:12100548] [WorldCat.org] [DOI] (P p)

Judita Mascarenhas, Jörg Soppa, Alexander V Strunnikov, Peter L Graumann
Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein.
EMBO J: 2002, 21(12);3108-18
[PubMed:12065423] [WorldCat.org] [DOI] (P p)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [WorldCat.org] [DOI] (P p)

V Azevedo, A Sorokin, S D Ehrlich, P Serror
The transcriptional organization of the Bacillus subtilis 168 chromosome region between the spoVAF and serA genetic loci.
Mol Microbiol: 1993, 10(2);397-405
[PubMed:7934830] [WorldCat.org] [DOI] (P p)