Difference between revisions of "EngA"

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Revision as of 13:46, 16 May 2013

  • Description: GTPase essential for ribosome 50S subunit assembly

Gene name yphC
Synonyms engA
Essential yes PubMed
Product GTPase
Function ribosome assembly
Gene expression levels in SubtiExpress: engA
MW, pI 48 kDa, 5.248
Gene length, protein length 1308 bp, 436 aa
Immediate neighbours gpsA, ypzH
Sequences Protein DNA DNA_with_flanks
Genetic context
YphC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YphC expression.png















Categories containing this gene/protein

translation, essential genes, GTP-binding proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU22840

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Binds and hydrolyzes GTP and readily exchanges GDP for GTP
  • Protein family: EngA subfamily (according to Swiss-Prot) Era/Obg family

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2HJG (complex with GDP)
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
    • for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP846, available in Jörg Stülke's lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Naotake Ogasawara, Nara, Japan

Your additional remarks

References

Reviews


Original publications

Anne-Emmanuelle Foucher, Jean-Baptiste Reiser, Christine Ebel, Dominique Housset, Jean-Michel Jault
Potassium acts as a GTPase-activating element on each nucleotide-binding domain of the essential Bacillus subtilis EngA.
PLoS One: 2012, 7(10);e46795
[PubMed:23056455] [WorldCat.org] [DOI] (I p)

Laura Schaefer, William C Uicker, Catherine Wicker-Planquart, Anne-Emmanuelle Foucher, Jean-Michel Jault, Robert A Britton
Multiple GTPases participate in the assembly of the large ribosomal subunit in Bacillus subtilis.
J Bacteriol: 2006, 188(23);8252-8
[PubMed:16997968] [WorldCat.org] [DOI] (P p)

Stephen P Muench, Ling Xu, Svetlana E Sedelnikova, David W Rice
The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding.
Proc Natl Acad Sci U S A: 2006, 103(33);12359-64
[PubMed:16894162] [WorldCat.org] [DOI] (P p)

Ling Xu, Stephen P Muench, Anna Roujeinikova, Svetlana E Sedelnikova, David W Rice
Cloning, purification and preliminary crystallographic analysis of the Bacillus subtilis GTPase YphC-GDP complex.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2006, 62(Pt 5);435-7
[PubMed:16682769] [WorldCat.org] [DOI] (I p)

Takuya Morimoto, Pek Chin Loh, Tomohiro Hirai, Kei Asai, Kazuo Kobayashi, Shigeki Moriya, Naotake Ogasawara
Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis.
Microbiology (Reading): 2002, 148(Pt 11);3539-3552
[PubMed:12427945] [WorldCat.org] [DOI] (P p)