RpmB

• Description: ribosomal protein
  
  

Gene name	rpmB
Synonyms	yloT
Essential	no PubMed
Product	ribosomal protein L28
Function	translation
Gene expression levels in SubtiExpress: rpmB
Interactions involving this protein in SubtInteract: RpmB
MW, pI	6 kDa, 12.242
Gene length, protein length	186 bp, 62 aa
Immediate neighbours	spoVM, yloU
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: BSU15820

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ribosomal protein L28P family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P37807

• KEGG entry: [2]

• E.C. number:

Additional information

• the protein is significantly underrepresented in 45S assembly intermediates that accumulate upon depletion of RbgA PubMed

Expression and regulation

• Operon:

• Expression browser: rpmB PubMed

• Sigma factor:

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed
  • strongly repressed in response to glucose starvation in M9 medium PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Ningning Li, Yuling Chen, Qiang Guo, Yixiao Zhang, Yi Yuan, Chengying Ma, Haiteng Deng, Jianlin Lei, Ning Gao
Cryo-EM structures of the late-stage assembly intermediates of the bacterial 50S ribosomal subunit.
Nucleic Acids Res: 2013, 41(14);7073-83
[PubMed:23700310] [WorldCat.org] [DOI] (I p)

Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921] [WorldCat.org] [DOI] (I p)

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)

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)