Difference between revisions of "OppA"

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(Biological materials)
(Biological materials)
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** BP67 (spc) available in [[Fabian Commichau]]'s lab
 
** BP67 (spc) available in [[Fabian Commichau]]'s lab
 
** 1S118 ( ''oppA''::''spec''), {{PubMed|11267663}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S118&Search=1S118 BGSC]
 
** 1S118 ( ''oppA''::''spec''), {{PubMed|11267663}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S118&Search=1S118 BGSC]
** GP2097 (D(''[[oppA]]-[[oppB]]-[[oppC]]-[[oppD]]-[[oppE]]'')::''aphA3''), available in [[Jörg Stülke]]'s lab
+
** GP2097 (D(''[[oppA]]-[[oppB]]-[[oppC]]-[[oppD]]-[[oppF]]'')::''aphA3''), available in [[Jörg Stülke]]'s lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 08:42, 20 July 2015

Gene name oppA
Synonyms spo0KA
Essential no
Product oligopeptide ABC transporter (binding protein)
Function initiation of sporulation, competence development
Gene expression levels in SubtiExpress: oppA
Interactions involving this protein in SubtInteract: OppA
Metabolic function and regulation of this protein in SubtiPathways:
OppA
MW, pI 61 kDa, 5.722
Gene length, protein length 1635 bp, 545 aa
Immediate neighbours trpS, oppB
Sequences Protein DNA DNA_with_flanks
Genetic context
OppA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
OppA expression.png















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

CodY regulon, 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:
    • required for the uptake of quorum sensing peptides such as PhrH PubMed
  • 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
  • Regulatory mechanism:
    • TnrA: transcription activation PubMed
    • ScoC: transcription repression PubMed
    • CodY: transcription repression, no derepression occurs, however, in a codY mutant, due to increased repression by ScoC PubMed
  • Additional information:
    • A ncRNA is predicted between trpS and oppA PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1937 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 20139 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Boris R Belitsky, Giulia Barbieri, Alessandra M Albertini, Eugenio Ferrari, Mark A Strauch, Abraham L Sonenshein
Interactive regulation by the Bacillus subtilis global regulators CodY and ScoC.
Mol Microbiol: 2015, 97(4);698-716
[PubMed:25966844] [WorldCat.org] [DOI] (I p)

Juri Niño Bach, Marc Bramkamp
Flotillins functionally organize the bacterial membrane.
Mol Microbiol: 2013, 88(6);1205-17
[PubMed:23651456] [WorldCat.org] [DOI] (I p)

Letal I Salzberg, Leagh Powell, Karsten Hokamp, Eric Botella, David Noone, Kevin M Devine
The WalRK (YycFG) and σ(I) RsgI regulators cooperate to control CwlO and LytE expression in exponentially growing and stressed Bacillus subtilis cells.
Mol Microbiol: 2013, 87(1);180-95
[PubMed:23199363] [WorldCat.org] [DOI] (I p)

Nicolas Mirouze, Vijay Parashar, Melinda D Baker, David A Dubnau, Matthew B Neiditch
An atypical Phr peptide regulates the developmental switch protein RapH.
J Bacteriol: 2011, 193(22);6197-206
[PubMed:21908671] [WorldCat.org] [DOI] (I p)

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)

D Z Rudner, J R LeDeaux, K Ireton, A D Grossman
The spo0K locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence.
J Bacteriol: 1991, 173(4);1388-98
[PubMed:1899858] [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)