Recombinant Bacillus subtilis ATP synthase subunit c (atpE)

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Description

Production and Purification

The recombinant protein is typically produced in E. coli with an N-terminal His tag for affinity purification . Key production parameters include:

  • Expression Host: E. coli (BL21 or similar strains).

  • Tag: Hexahistidine (His-tag) for immobilized metal ion affinity chromatography (IMAC) .

  • Purity: >90% as confirmed by SDS-PAGE .

Table 3: Key Research Findings

Study FocusFindingsSource
ε Subunit InteractionC-terminal α-helices of ε inhibit ATPase activity by stabilizing the c-ring .
Antibiotic TargetingMutations in atpE (e.g., V48I, V60A) confer resistance to diarylquinolines .
Assembly RequirementsAtpI chaperone assists c-ring assembly in Na+^+-coupled ATP synthases but is nonessential in B. subtilis .

Applications in Research

  • Drug Development: AtpE is a validated target for novel antibiotics (e.g., diarylquinolines) due to its conserved structure in pathogenic bacteria .

  • Structural Studies: Recombinant AtpE facilitates cryo-EM and X-ray crystallography studies of c-ring architecture .

Table 4: Antibiotic Resistance Mutations in AtpE

MutationEffect on Drug BindingPathogen Affected
V48ISteric hindrance reduces inhibitor efficacyStreptococcus pneumoniae
V60AAlters proton channel conformationStaphylococcus aureus

Future Directions

  • Mechanistic Studies: Elucidate the role of conserved residues (e.g., E56) in proton coupling .

  • Industrial Applications: Engineer thermostable AtpE variants for bioenergy applications .

Product Specs

Form
Lyophilized powder
Please note: We will prioritize shipping the format currently in stock. However, if you require a specific format, please indicate your preference in the order notes. We will fulfill your request whenever possible.
Lead Time
Delivery time may vary depending on the purchase method and location. For specific delivery timelines, please consult your local distributor.
Please note: All protein shipments are standardly packaged with blue ice packs. If you require dry ice packaging, please contact us in advance for arrangements and associated fees.
Notes
Repeated freezing and thawing is not recommended. For optimal use, store working aliquots at 4°C for up to one week.
Reconstitution
We recommend centrifuging the vial briefly before opening to ensure the contents settle at the bottom. Please reconstitute the protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. We suggest adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default glycerol final concentration is 50%, which can be used as a reference.
Shelf Life
Shelf life is influenced by various factors including storage conditions, buffer components, temperature, and the intrinsic stability of the protein.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during the manufacturing process.
The tag type will be determined during the production process. If you require a specific tag type, please inform us, and we will prioritize its inclusion during development.
Synonyms
atpE; BSU36860; ATP synthase subunit c; ATP synthase F(0 sector subunit c; F-type ATPase subunit c; F-ATPase subunit c; Lipid-binding protein
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-70
Protein Length
full length protein
Species
Bacillus subtilis (strain 168)
Target Names
atpE
Target Protein Sequence
MNLIAAAIAIGLGALGAGIGNGLIVSRTVEGIARQPEAGKELRTLMFMGIALVEALPIIA VVIAFLAFFG
Uniprot No.

Target Background

Function
F(1)F(0) ATP synthase generates ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases comprise two structural domains: F(1) encompassing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked by a central stalk and a peripheral stalk. During catalysis, ATP synthesis within the catalytic domain of F(1) is coupled to proton translocation via a rotary mechanism involving the central stalk subunits. This subunit is a key component of the F(0) channel and directly participates in translocation across the membrane. A homomeric c-ring, composed of 10-14 subunits, forms the central stalk rotor element in conjunction with the F(1) delta and epsilon subunits.
Database Links
Protein Families
ATPase C chain family
Subcellular Location
Cell membrane; Multi-pass membrane protein.

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