OppA

• Description: oligopeptide ABC transporter (binding protein)
  
  

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
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:
  • (OppD-OppF)-(OppB-OppC)-OppA PubMed
  • FloT-OppA PubMed

• Localization:
  • attached to the cell membrane (via OppB-OppC) PubMed
  • at the outer side of the cell: extracellular (signal peptide) PubMed, lipid modification as retention signal PubMed

Database entries

• Structure:

• UniProt: P24141

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: oppA-oppB-oppC-oppD-oppF PubMed

• Expression browser: oppA PubMed

• Sigma factor:

• 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

• Additional information:
  • A ncRNA is predicted between trpS and oppA PubMed

Biological materials

• Mutant: BP67 (spc) available in Fabian Commichau's lab
  • 1S118 ( oppA::spec), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

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)