ScpA

• Description: part of the condensin complex, chromosomal origin condensation and segregation
  
  

Gene name	scpA
Synonyms	ypuG
Essential	yes PubMed
Product	DNA segregation and condensation protein
Function	segregation of replication origins
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
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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
• scpA mutants are not viable on complex medim that allow rapid growth, but they are viable under conditions of slow growth PubMed

Database entries

• BsubCyc: BSU23220

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • part of the condensin complex PubMed
  • present as stable monomer PubMed
  • ScpA-Smc PubMed
  • ScpA-ScpB PubMed

• Localization:
  • nucleoid (Multiple) PubMed
  • the condensin (Smc)2-ScpA-ScpB complex forms two bipolar assemblies on the chromosome, one in each cell half, localization depends on Spo0J PubMed

Database entries

• BsubCyc: BSU23220

• 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
  • 4I98 (complex between ScpA (aa 1-160)-ScpB (aa 1-183) PubMed

• UniProt: P35154

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: scpA-scpB-ypuI PubMed

• Expression browser: scpA PubMed

• Sigma factor:

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

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 573 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 1071 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Stephan Gruber, Jan-Willem Veening, Juri Bach, Martin Blettinger, Marc Bramkamp, Jeff Errington
Interlinked sister chromosomes arise in the absence of condensin during fast replication in B. subtilis.
Curr Biol: 2014, 24(3);293-8
[PubMed:24440399] [WorldCat.org] [DOI] (I p)

Xindan Wang, Olive W Tang, Eammon P Riley, David Z Rudner
The SMC condensin complex is required for origin segregation in Bacillus subtilis.
Curr Biol: 2014, 24(3);287-92
[PubMed:24440393] [WorldCat.org] [DOI] (I p)

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)

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)