Difference between revisions of "ScpB"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ypuI]]'', ''[[scpA]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ypuI]]'', ''[[scpA]]''
 
|-
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU23210 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU23210 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU23210 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU23210 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU23210 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU23210 DNA_with_flanks]
 
|-
 
|-
 
|colspan="2" | '''Genetic context''' <br/> [[Image:ypuH_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:ypuH_context.gif]]

Revision as of 10:36, 14 May 2013

  • Description: DNA segregation and condensation protein

Gene name scpB
Synonyms ypuH
Essential no
Product DNA segregation and condensation protein
Function maintenance of chromosome structure
Gene expression levels in SubtiExpress: scpB
Interactions involving this protein in SubtInteract: ScpB
MW, pI 21 kDa, 4.25
Gene length, protein length 591 bp, 197 aa
Immediate neighbours ypuI, scpA
Sequences Protein DNA DNA_with_flanks
Genetic context
YpuH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ScpB expression.png















Categories containing this gene/protein

DNA condensation/ segregation

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU23210

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: scpB 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

  • 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

Additional publications: PubMed

Luise A K Kleine Borgmann, Hanna Hummel, Maximilian H Ulbrich, Peter L Graumann
SMC condensation centers in Bacillus subtilis are dynamic structures.
J Bacteriol: 2013, 195(10);2136-45
[PubMed:23475963] [WorldCat.org] [DOI] (I p)

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)

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)

A Volkov, J Mascarenhas, C Andrei-Selmer, H D Ulrich, P L Graumann
A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure.
Mol Cell Biol: 2003, 23(16);5638-50
[PubMed:12897137] [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)