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

• 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

• 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

Additional publications: PubMed

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)

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)