Difference between revisions of "OppA"

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(Extended information on the protein)
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' ([[OppD]]-[[OppF]])-([[OppB]]-[[OppC]])-[[OppA]] {{PubMed|10092453}}
+
* '''[[SubtInteract|Interactions]]:'''
 +
**  ([[OppD]]-[[OppF]])-([[OppB]]-[[OppC]])-[[OppA]] {{PubMed|10092453}}
  
* '''Localization:'''  
+
* '''[[Localization]]:'''  
 
** attached to the cell membrane (via [[OppB]]-[[OppC]]) {{PubMed|10092453}}
 
** attached to the cell membrane (via [[OppB]]-[[OppC]]) {{PubMed|10092453}}
 
** at the outer side of the cell: extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed],  lipid modification as retention signal [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
 
** at the outer side of the cell: extracellular (signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed],  lipid modification as retention signal [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]

Revision as of 14:38, 10 August 2011

Gene name oppA
Synonyms spo0KA
Essential no
Product oligopeptide ABC transporter (binding protein)
Function initiation of sporulation, competence development
Interactions involving this protein in SubtInteract: OppA
MW, pI 61 kDa, 5.722
Gene length, protein length 1635 bp, 545 aa
Immediate neighbours trpS, oppB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
OppA context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

ABC transporters, utilization of nitrogen sources other than amino acids, genetic competence, phosphorelay, membrane proteins

This gene is a member of the following regulons

ScoC regulon, TnrA regulon

The gene

Basic information

  • Locus tag: BSU11430

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: bacterial solute-binding protein 5 family (according to Swiss-Prot)
  • Paralogous protein(s): DppE

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on (Tyr-301 OR Tyr-303) AND Thr-470 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • expressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
    • repressed during exponential growth (ScoC) PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818] [WorldCat.org] [DOI] (P p)

A Yazgan, G Ozcengiz, M A Marahiel
Tn10 insertional mutations of Bacillus subtilis that block the biosynthesis of bacilysin.
Biochim Biophys Acta: 2001, 1518(1-2);87-94
[PubMed:11267663] [WorldCat.org] [DOI] (P p)

M S Turner, J D Helmann
Mutations in multidrug efflux homologs, sugar isomerases, and antimicrobial biosynthesis genes differentially elevate activity of the sigma(X) and sigma(W) factors in Bacillus subtilis.
J Bacteriol: 2000, 182(18);5202-10
[PubMed:10960106] [WorldCat.org] [DOI] (P p)

A Koide, M Perego, J A Hoch
ScoC regulates peptide transport and sporulation initiation in Bacillus subtilis.
J Bacteriol: 1999, 181(13);4114-7
[PubMed:10383984] [WorldCat.org] [DOI] (P p)

Y Quentin, G Fichant, F Denizot
Inventory, assembly and analysis of Bacillus subtilis ABC transport systems.
J Mol Biol: 1999, 287(3);467-84
[PubMed:10092453] [WorldCat.org] [DOI] (P p)

J R LeDeaux, J M Solomon, A D Grossman
Analysis of non-polar deletion mutations in the genes of the spo0K (opp) operon of Bacillus subtilis.
FEMS Microbiol Lett: 1997, 153(1);63-9
[PubMed:9252573] [WorldCat.org] [DOI] (P p)

A Koide, J A Hoch
Identification of a second oligopeptide transport system in Bacillus subtilis and determination of its role in sporulation.
Mol Microbiol: 1994, 13(3);417-26
[PubMed:7997159] [WorldCat.org] [DOI] (P p)

M Perego, C F Higgins, S R Pearce, M P Gallagher, J A Hoch
The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation.
Mol Microbiol: 1991, 5(1);173-85
[PubMed:1901616] [WorldCat.org] [DOI] (P p)