Recombinant Bacillus cereus ATP synthase subunit beta (atpD)

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Description

Structure and Function

The F₀F₁ ATP synthase in Bacillus species consists of two main components:

  • F₀: A membrane-bound proton channel (subunits a, b, c, and others).

  • F₁: A soluble catalytic domain (subunits α, β, γ, δ, ε).

AtpD encodes the β-subunit of F₀, which plays a structural role in proton translocation and ATP synthesis. In B. subtilis, atpD expression is linked to oxidative phosphorylation efficiency, with its deletion impairing ATP production . While B. cereus atpD-specific studies are absent in provided sources, its functional homology to B. subtilis atpD suggests analogous roles.

Role in Bacillus cereus Metabolism

AtpD likely contributes to:

  • Oxidative phosphorylation: Generating ATP during aerobic respiration.

  • Stress responses: Acid resistance mechanisms, as shown by upregulation of F₁ ATP synthase subunits (e.g., atpB) during low-pH environments .

  • Redox regulation: Interactions with proteins like Rex, which modulates metabolic pathways in response to NADH/NAD⁺ ratios .

Experimental and Recombinant Applications

Recombinant atpD production involves heterologous expression systems (e.g., E. coli) for structural or functional studies. Such constructs enable:

  • Biochemical assays to measure proton translocation efficiency or ATP synthesis rates.

  • Proteomic analysis of stress-induced modifications (e.g., phosphorylation, redox-sensitive residues) .

Research Findings and Implications

Study FocusKey FindingsRelevance to AtpD
Oxidative phosphorylationDeletion of BsuMI in B. subtilis reduces oxidative phosphorylation efficiency .Suggests atpD homologs in B. cereus may similarly regulate ATP production under stress.
Acid resistance mechanismsB. cereus upregulates F₁ ATP synthase (atpB) during acid shock .Indicates F₀ subunits like atpD may complement acid-resistance ATP synthesis pathways.
Rex-mediated regulationRex controls metabolic fluxes, including lactate fermentation and respiration .AtpD may be indirectly regulated by Rex during metabolic shifts.

Product Specs

Form
Lyophilized powder. We will ship the in-stock format. If you have special format requirements, please note them when ordering, and we will fulfill your request.
Lead Time
Delivery times vary by purchase method and location. Consult your local distributor for specific delivery times. All proteins are shipped with standard blue ice packs. For dry ice shipping, contact us in advance; additional charges apply.
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening to collect contents at the bottom. Reconstitute the protein in sterile deionized water to 0.1-1.0 mg/mL. Add 5-50% glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on storage conditions, buffer components, storage temperature, and protein stability. Liquid form shelf life is typically 6 months at -20°C/-80°C. Lyophilized form shelf life is typically 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type is determined during manufacturing. If you require a specific tag, please inform us, and we will prioritize its development.
Synonyms
atpD; BCQ_5145ATP synthase subunit beta; EC 7.1.2.2; ATP synthase F1 sector subunit beta; F-ATPase subunit beta
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-468
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Bacillus cereus (strain Q1)
Target Names
atpD
Target Protein Sequence
MNKGRVTQIM GPVVDVKFDG GKLPEIYNAL TVKQSNENGE LNLTFEVALH LGDDTVRTVA MSSTDGLVRG TEVEDTGKAI SVPVGDATLG RVFNVLGDAI DLDGEVPADV RRDPIHRQAP AFEELSTKVE ILETGIKVVD LLAPYIKGGK IGLFGGAGVG KTVLIQELIN NIAQEHGGIS VFAGVGERTR EGNDLYHEMS DSGVIKKTAM VFGQMNEPPG ARQRVALTGL TMAEYFRDEQ GQDVLLFIDN IFRFTQAGSE VSALLGRMPS AVGYQPTLAT EMGQLQERIT STNKGSITSI QAVYVPADDY TDPAPATTFA HLDATTNLER RLTQMGIYPA VDPLASTSRA LSPEIVGEEH YEVARQVQQT LQRYKELQDI IAILGMDELS EEDKLVVHRA RRIQFFLSQN FHVAEQFTGQ KGSYVPVKDT VRGFKEILEG KYDDLPEDAF RLVGGIEEVI ENAKKMMA
Uniprot No.

Target Background

Function
Generates ATP from ADP using a proton gradient across the membrane. The catalytic sites are mainly located in the beta subunits.
Database Links

KEGG: bcq:BCQ_5145

Protein Families
ATPase alpha/beta chains family
Subcellular Location
Cell membrane; Peripheral membrane protein.

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