RpmA

• Description: ribosomal protein
  
  

Gene name	rpmA
Synonyms
Essential	yes PubMed
Product	ribosomal protein L27 (BL24)
Function	translation
Gene expression levels in SubtiExpress: rpmA
Interactions involving this protein in SubtInteract: RpmA
MW, pI	10 kDa, 10.764
Gene length, protein length	282 bp, 94 aa
Immediate neighbours	spo0B, prp
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

The gene

Basic information

• Locus tag: BSU27940

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU27940

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ribosomal protein L27P family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • the N-terminal extension is cleaved off by Prp PubMed
• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU27940

• Structure:

• UniProt: P05657

• KEGG entry: [3]

• 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: rpmA PubMed

• Expression browser: rpmA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 650 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 1644 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Erin A Wall, J Harry Caufield, Charles E Lyons, Keith A Manning, Terje Dokland, Gail E Christie
Specific N-terminal cleavage of ribosomal protein L27 in Staphylococcus aureus and related bacteria.
Mol Microbiol: 2015, 95(2);258-69
[PubMed:25388641] [WorldCat.org] [DOI] (I p)

Ahmad Jomaa, Nikhil Jain, Joseph H Davis, James R Williamson, Robert A Britton, Joaquin Ortega
Functional domains of the 50S subunit mature late in the assembly process.
Nucleic Acids Res: 2014, 42(5);3419-35
[PubMed:24335279] [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)

A Wipat, N Carter, S C Brignell, B J Guy, K Piper, J Sanders, P T Emmerson, C R Harwood
The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism.
Microbiology (Reading): 1996, 142 ( Pt 11);3067-78
[PubMed:8969504] [WorldCat.org] [DOI] (P p)