Recombinant Elusimicrobium minutum ATP synthase subunit b (atpF)

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Description

Key Features of E. minutum Metabolism

FeatureDescription
Anaerobic FermentationD-galactose, D-glucose, and D-fructose are fermented to acetate, ethanol, H₂, and alanine .
Energy CouplingHydrogenases and peptidoglycan synthesis genes are present, but ATP synthase subunits are not explicitly annotated .
Recombinant Protein PotentialGenomic data hint at biosynthetic pathways (e.g., polyketide synthesis) and secretion systems, suggesting capacity for recombinant protein production .

Role of ATP Synthase Subunit b (atpF) in Bacterial Systems

Subunit b is part of the F₀ sector of F-type ATP synthases, critical for proton translocation and ATP synthesis. In other bacteria (e.g., Thermobifida fusca, Bacillus pumilus), recombinant subunit b proteins have been expressed in E. coli for structural and functional studies . Key functions include:

  • Proton Channel Formation: Subunit b contributes to the proton pathway in the F₀ complex.

  • Stability and Assembly: Interacts with subunits a and c to form the membrane-bound F₀ sector .

Recombinant Protein Production in Bacteria

OrganismSubunit b ExpressionSource
Thermobifida fuscaFull-length His-tagged protein (1–179 aa) expressed in E. coli .
Bacillus pumilusFull-length His-tagged protein (1–170 aa) with >90% purity .

Potential Research Directions

  1. Genetic Engineering: Recombinant expression of E. minutum atpF in E. coli to study subunit interactions and proton translocation.

  2. Biochemical Characterization: Kinetic analysis of ATP synthase activity in E. minutum membrane fractions.

  3. Phylogenetic Analysis: Comparative genomics to identify conserved motifs in E. minutum atpF homologs.

Challenges and Knowledge Gaps

  • Limited Annotation: ATP synthase subunits are not explicitly annotated in E. minutum genomes, requiring bioinformatics tools to identify homologs .

  • Recombinant Protein Data: No published studies describe the cloning, expression, or purification of E. minutum atpF.

  • Metabolic Context: The role of ATP synthase in E. minutum’s reductive acetogenesis or hydrogen metabolism remains unexplored .

Product Specs

Form
Lyophilized powder
Note: While we prioritize shipping the format currently in stock, please specify your format preference in order notes for customized preparation.
Lead Time
Delivery times vary depending on the purchase method and location. Please consult your local distributor for precise delivery estimates.
Note: Standard shipping includes blue ice packs. Dry ice shipping requires prior arrangement and incurs additional charges.
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Centrifuge the vial briefly before opening to collect the contents. Reconstitute the protein in sterile, deionized water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our standard glycerol concentration is 50% and can serve as a guideline.
Shelf Life
Shelf life depends on several factors including storage conditions, buffer composition, temperature, and protein stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized formulations have a 12-month shelf life at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type is determined during the manufacturing process.
If you require a specific tag, please inform us, and we will prioritize its development.
Synonyms
atpF; Emin_1517; ATP synthase subunit b; ATP synthase F(0 sector subunit b; ATPase subunit I; F-type ATPase subunit b; F-ATPase subunit b
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-165
Protein Length
full length protein
Species
Elusimicrobium minutum (strain Pei191)
Target Names
atpF
Target Protein Sequence
MNALLTPDYGLIFWTIVNFLLLVFLLGKFAWKPIIGALEARENKISQDKKDAQEARDEAQ KIKAELDVRLSNISKEAQEKLAQVEALAKQQKDAMIKDAQASSERMIATAKEEIEAQKNQ ALKEVKKEIADMAVEAAAKIAGVKTDPKTDAALVDNIVKDIINKA
Uniprot No.

Target Background

Function

F1F0 ATP synthase synthesizes ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases comprise two structural domains: F1, containing the extramembranous catalytic core; and F0, containing the membrane proton channel. These domains are linked by a central stalk and a peripheral stalk. ATP synthesis in the F1 catalytic domain is coupled, via a rotary mechanism of the central stalk subunits, to proton translocation. This protein is a component of the F0 channel, forming part of the peripheral stalk that connects F1 and F0.

Database Links
Protein Families
ATPase B chain family
Subcellular Location
Cell membrane; Single-pass membrane protein.

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