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

Additional publications: PubMed

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)