EngA

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  • 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, seaA
Get the DNA and protein sequences
(Barbe et al., 2009)
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

Natalie Verstraeten, Maarten Fauvart, Wim Versées, Jan Michiels
The universally conserved prokaryotic GTPases.
Microbiol Mol Biol Rev: 2011, 75(3);507-42, second and third pages of table of contents
[PubMed:21885683] [WorldCat.org] [DOI] (I p)

Robert A Britton
Role of GTPases in bacterial ribosome assembly.
Annu Rev Microbiol: 2009, 63;155-76
[PubMed:19575570] [WorldCat.org] [DOI] (I p)


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)