EngA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation, essential genes, GTP-binding proteins

The gene

Basic information

• Locus tag: BSU22840

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU22840

• DBTBS entry: no entry

• SubtiList entry: [1]

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

• Paralogous protein(s): Era, Obg, YsxC, RbgA, YqeH, ThdF, YyaF, YnbA

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU22840

• Structure: 2HJG (complex with GDP)

• UniProt: P50743

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: engA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 225 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 935 PubMed

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

References

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)