Smc

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

Gene name	smc
Synonyms	ylqA
Essential	yes PubMed
Product	chromosome condensation and segregation SMC protein
Function	segregation of replication origins
Gene expression levels in SubtiExpress: smc
Interactions involving this protein in SubtInteract: Smc
Metabolic function and regulation of this protein in SubtiPathways: Smc
MW, pI	135 kDa, 5.266
Gene length, protein length	3558 bp, 1186 aa
Immediate neighbours	rnc, ftsY
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

The gene

Basic information

• Locus tag: BSU15940

Phenotypes of a mutant

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

Database entries

• BsubCyc: BSU15940

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: SMC family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:
  • ATP-induced DNA-binding results in a more open conformation of the Smc dimer, and thus of the condension complex PubMed

• Interactions:
  • part of the condensin complex PubMed
  • forms dimers PubMed
  • ScpA-Smc PubMed
  • ScpB-Smc, PubMed, this interaction takes place only in the presence of ScpA PubMed
  • Smc is a member of a suspected group of hubs proteins that were suggested to be involved in a large number of interactions PubMed

• Localization:
  • nucleoid (heterogeneous) 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: BSU15940

• 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

• UniProt: P51834

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: rnc-smc-ftsY PubMed

• Expression browser: smc PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:
  • 1A822 ( smc::erm), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Xindan Wang, Tung B K Le, Bryan R Lajoie, Job Dekker, Michael T Laub, David Z Rudner
Condensin promotes the juxtaposition of DNA flanking its loading site in Bacillus subtilis.
Genes Dev: 2015, 29(15);1661-75
[PubMed:26253537] [WorldCat.org] [DOI] (I p)

Larissa Wilhelm, Frank Bürmann, Anita Minnen, Ho-Chul Shin, Christopher P Toseland, Byung-Ha Oh, Stephan Gruber
SMC condensin entraps chromosomal DNA by an ATP hydrolysis dependent loading mechanism in Bacillus subtilis.
Elife: 2015, 4;
[PubMed:25951515] [WorldCat.org] [DOI] (I e)

Vincent M Waldman, Tyler H Stanage, Alexandra Mims, Ian S Norden, Martha G Oakley
Structural mapping of the coiled-coil domain of a bacterial condensin and comparative analyses across all domains of life suggest conserved features of SMC proteins.
Proteins: 2015, 83(6);1027-45
[PubMed:25664627] [WorldCat.org] [DOI] (I p)

Young-Min Soh, Frank Bürmann, Ho-Chul Shin, Takashi Oda, Kyeong Sik Jin, Christopher P Toseland, Cheolhee Kim, Hansol Lee, Soo Jin Kim, Min-Seok Kong, Marie-Laure Durand-Diebold, Yeon-Gil Kim, Ho Min Kim, Nam Ki Lee, Mamoru Sato, Byung-Ha Oh, Stephan Gruber
Molecular basis for SMC rod formation and its dissolution upon DNA binding.
Mol Cell: 2015, 57(2);290-303
[PubMed:25557547] [WorldCat.org] [DOI] (I p)

Xindan Wang, Paula Montero Llopis, David Z Rudner
Bacillus subtilis chromosome organization oscillates between two distinct patterns.
Proc Natl Acad Sci U S A: 2014, 111(35);12877-82
[PubMed:25071173] [WorldCat.org] [DOI] (I p)

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)

Elodie Marchadier, Rut Carballido-López, Sophie Brinster, Céline Fabret, Peggy Mervelet, Philippe Bessières, Marie-Françoise Noirot-Gros, Vincent Fromion, Philippe Noirot
An expanded protein-protein interaction network in Bacillus subtilis reveals a group of hubs: Exploration by an integrative approach.
Proteomics: 2011, 11(15);2981-91
[PubMed:21630458] [WorldCat.org] [DOI] (I p)

Nora L Sullivan, Kathleen A Marquis, David Z Rudner
Recruitment of SMC by ParB-parS organizes the origin region and promotes efficient chromosome segregation.
Cell: 2009, 137(4);697-707
[PubMed:19450517] [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)

Robert A Britton, Elke Küster-Schöck, Thomas A Auchtung, Alan D Grossman
SOS induction in a subpopulation of structural maintenance of chromosome (Smc) mutant cells in Bacillus subtilis.
J Bacteriol: 2007, 189(12);4359-66
[PubMed:17416649] [WorldCat.org] [DOI] (P 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)

P L Graumann, R Losick
Coupling of asymmetric division to polar placement of replication origin regions in Bacillus subtilis.
J Bacteriol: 2001, 183(13);4052-60
[PubMed:11395470] [WorldCat.org] [DOI] (P p)

P L Graumann, R Losick, A V Strunnikov
Subcellular localization of Bacillus subtilis SMC, a protein involved in chromosome condensation and segregation.
J Bacteriol: 1998, 180(21);5749-55
[PubMed:9791128] [WorldCat.org] [DOI] (P p)