RpmE

• Description: ribosomal protein
  
  

Gene name	rpmE
Synonyms
Essential	no PubMed
Product	ribosomal protein L31
Function	translation
Gene expression levels in SubtiExpress: rpmE
Interactions involving this protein in SubtInteract: RpmE
MW, pI	7 kDa, 9.157
Gene length, protein length	198 bp, 66 aa
Immediate neighbours	tdk, rho
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

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU37070

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: Type A subfamily (according to Swiss-Prot)

• Paralogous protein(s): YtiA

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity: Zn(2+) PubMed

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: Q03223

• KEGG entry: [3]

• E.C. number:

Additional information

Under conditions of zinc starvation, RpmE is replaced by its paralog YtiA, that does not require zinc PubMed

Expression and regulation

• Operon: rpmE PubMed

• Expression browser: rpmE PubMed

• Sigma factor:

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Genki Akanuma, Hideaki Nanamiya, Yousuke Natori, Koichi Yano, Shota Suzuki, Shuya Omata, Morio Ishizuka, Yasuhiko Sekine, Fujio Kawamura
Inactivation of ribosomal protein genes in Bacillus subtilis reveals importance of each ribosomal protein for cell proliferation and cell differentiation.
J Bacteriol: 2012, 194(22);6282-91
[PubMed:23002217] [WorldCat.org] [DOI] (I p)

Hideaki Nanamiya, Fujio Kawamura
Towards an elucidation of the roles of the ribosome during different growth phases in Bacillus subtilis.
Biosci Biotechnol Biochem: 2010, 74(3);451-61
[PubMed:20208344] [WorldCat.org] [DOI] (I p)

Matthew A Lauber, William E Running, James P Reilly
B. subtilis ribosomal proteins: structural homology and post-translational modifications.
J Proteome Res: 2009, 8(9);4193-206
[PubMed:19653700] [WorldCat.org] [DOI] (P p)

Scott E Gabriel, John D Helmann
Contributions of Zur-controlled ribosomal proteins to growth under zinc starvation conditions.
J Bacteriol: 2009, 191(19);6116-22
[PubMed:19648245] [WorldCat.org] [DOI] (I p)

Yousuke Natori, Hideaki Nanamiya, Genki Akanuma, Saori Kosono, Toshiaki Kudo, Kozo Ochi, Fujio Kawamura
A fail-safe system for the ribosome under zinc-limiting conditions in Bacillus subtilis.
Mol Microbiol: 2007, 63(1);294-307
[PubMed:17163968] [WorldCat.org] [DOI] (P p)

Hideaki Nanamiya, Genki Akanuma, Yousuke Natori, Rikinori Murayama, Saori Kosono, Toshiaki Kudo, Kazuo Kobayashi, Naotake Ogasawara, Seung-Moon Park, Kozo Ochi, Fujio Kawamura
Zinc is a key factor in controlling alternation of two types of L31 protein in the Bacillus subtilis ribosome.
Mol Microbiol: 2004, 52(1);273-83
[PubMed:15049826] [WorldCat.org] [DOI] (P p)