ScpB

From SubtiWiki
Revision as of 11:38, 17 September 2009 by Jstuelk (talk | contribs) (Extended information on the protein)
Jump to: navigation, search
  • Description: DNA segregation and condensation protein

Gene name scpB
Synonyms ypuH
Essential no
Product DNA segregation and condensation protein
Function maintenance of chromosome structure
MW, pI 21 kDa, 4.25
Gene length, protein length 591 bp, 197 aa
Immediate neighbours ypuI, scpA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YpuH context.gif
This image was kindly provided by SubtiList



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:
  • Localization: Nucleoid (Multiple) PubMed

Database entries

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

Additional information

Expression and regulation

  • Operon:
  • 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

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)