RplA

• Description: ribosomal protein
  
  

Gene name	rplA
Synonyms
Essential	no PubMed
Product	ribosomal protein L1 (BL1)
Function	translation
Gene expression levels in SubtiExpress: rplA
Interactions involving this protein in SubtInteract: RplA
MW, pI	24 kDa, 9.732
Gene length, protein length	696 bp, 232 aa
Immediate neighbours	rplK, rplJ
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, universally conserved proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU01030

Database entries

• BsubCyc: BSU01030

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: ribosomal protein L1P family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • YsxC-RplA PubMed
  • RplA-CshA PubMed

• Localization:

Database entries

• BsubCyc: BSU01030

• Structure:

• UniProt: Q06797

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: rplA PubMed

• Sigma factor:

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed
  • expression transiently increases in the forespore PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

• FLAG-tag construct:
  • GP1094 (erm, based on pGP1087), available in Jörg Stülke's lab

• Antibody:

References

Martin Lehnik-Habrink, Leonie Rempeters, Ákos T Kovács, Christoph Wrede, Claudia Baierlein, Heike Krebber, Oscar P Kuipers, Jörg Stülke
DEAD-Box RNA helicases in Bacillus subtilis have multiple functions and act independently from each other.
J Bacteriol: 2013, 195(3);534-44
[PubMed:23175651] [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)

Alex Rosenberg, Lior Sinai, Yoav Smith, Sigal Ben-Yehuda
Dynamic expression of the translational machinery during Bacillus subtilis life cycle at a single cell level.
PLoS One: 2012, 7(7);e41921
[PubMed:22848659] [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)

Catherine Wicker-Planquart, Anne-Emmanuelle Foucher, Mathilde Louwagie, Robert A Britton, Jean-Michel Jault
Interactions of an essential Bacillus subtilis GTPase, YsxC, with ribosomes.
J Bacteriol: 2008, 190(2);681-90
[PubMed:17981968] [WorldCat.org] [DOI] (I p)

J Mascarenhas, M H Weber, P L Graumann
Specific polar localization of ribosomes in Bacillus subtilis depends on active transcription.
EMBO Rep: 2001, 2(8);685-9
[PubMed:11463749] [WorldCat.org] [DOI] (P p)