Difference between revisions of "SecA"

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[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:09, 23 November 2012

  • Description: preprotein translocase subunit (ATPase)

Gene name secA
Synonyms div, div-341, ts-341
Essential yes PubMed
Product preprotein translocase subunit (ATPase)
Function protein secretion
Gene expression levels in SubtiExpress: secA
Interactions involving this protein in SubtInteract: SecA
Metabolic function and regulation of this protein in SubtiPathways:
Protein secretion
MW, pI 95 kDa, 5.34
Gene length, protein length 2523 bp, 841 aa
Immediate neighbours prfB, yvyD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SecA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SecA expression.png















Categories containing this gene/protein

protein secretion, essential genes, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU35300

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: ATP -> ADP + Pi + preprotein translocation
  • Protein family: SecA family (according to Swiss-Prot)
  • Paralogous protein(s): none in Bacillus, some species have a paralogous secA gene named secA2 that has an altered substrate range

Extended information on the protein

  • Kinetic information:
  • Domains: nucleotide binding domain, preprotein binding domain, IRA2 domain, scaffold domain, wing domain, IRA1 domain, C-terminal domain
  • Modification:
  • Cofactor(s): magnesium
  • Effectors of protein activity: anionic phospholipids, preprotein, SecY, signal peptides (even when added in trans) PubMed

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Dorothy M Kim, Haiyan Zheng, Yuanpeng J Huang, Gaetano T Montelione, John F Hunt
ATPase active-site electrostatic interactions control the global conformation of the 100 kDa SecA translocase.
J Am Chem Soc: 2013, 135(8);2999-3010
[PubMed:23167435] [WorldCat.org] [DOI] (I p)

Hiroshi Kakeshita, Yasushi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Kouji Nakamura
Enhanced extracellular production of heterologous proteins in Bacillus subtilis by deleting the C-terminal region of the SecA secretory machinery.
Mol Biotechnol: 2010, 46(3);250-7
[PubMed:20574771] [WorldCat.org] [DOI] (I p)

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

Jan D H Jongbloed, Haike Antelmann, Michael Hecker, Reindert Nijland, Sierd Bron, Ulla Airaksinen, Frens Pries, Wim J Quax, Jan Maarten van Dijl, Peter G Braun
Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis.
J Biol Chem: 2002, 277(46);44068-78
[PubMed:12218047] [WorldCat.org] [DOI] (P p)

M Herbort, M Klein, E H Manting, A J Driessen, R Freudl
Temporal expression of the Bacillus subtilis secA gene, encoding a central component of the preprotein translocase.
J Bacteriol: 1999, 181(2);493-500
[PubMed:9882663] [WorldCat.org] [DOI] (P p)

K Bunai, K Yamada, K Hayashi, K Nakamura, K Yamane
Enhancing effect of Bacillus subtilis Ffh, a homologue of the SRP54 subunit of the mammalian signal recognition particle, on the binding of SecA to precursors of secretory proteins in vitro.
J Biochem: 1999, 125(1);151-9
[PubMed:9880811] [WorldCat.org] [DOI] (P p)

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