Recombinant Mycobacterium gilvum ATP synthase subunit beta (atpD)

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Description

Recombinant Expression Systems in Mycobacteria

Studies on recombinant ATP synthase subunits in other mycobacteria provide a framework for understanding potential applications for M. gilvum atpD:

Key Research Findings

FeatureM. tuberculosis atpDM. smegmatis atpDM. gilvum (Inferred)
Catalytic efficiencyLatent ATPase activity Enhanced hydrolysis in αCTD mutants Likely regulated by αCTD/γ-loop analogs
Structural motifsγ-loop (14 aa insert) γ-loop critical for ATP synthesis Uncharacterized
Recombinant studiesUsed for drug target validation Cryo-EM structures resolved No published structures
  • Heterologous expression: Recombinant atpD from M. tuberculosis and M. smegmatis has been expressed in E. coli or mycobacterial vectors for functional assays .

  • Regulatory elements: The αCTD in M. smegmatis suppresses ATP hydrolysis, a mechanism potentially conserved in M. gilvum .

Potential Applications and Research Gaps

While M. gilvum is a nonpathogenic, bioremediation-relevant species, its ATP synthase remains understudied.

Inferred Insights

  • Biotechnological utility: Recombinant atpD could enable studies on:

    • ATP synthase inhibition strategies for related pathogens .

    • Metabolic engineering for enhanced ATP yield in synthetic biology applications.

  • Comparative genomics: M. gilvum shares evolutionary traits with pathogenic mycobacteria, including horizontal gene transfer (HGT) events linked to metabolic adaptation .

Critical Challenges and Future Directions

  1. Structural characterization: No cryo-EM or crystallographic data exist for M. gilvum F-ATP synthase.

  2. Functional assays: ATP hydrolysis/synthesis kinetics of recombinant atpD remain untested.

  3. Evolutionary context: Horizontal acquisition of ATP synthase-related genes in mycobacteria (e.g., moaA1-D1 locus in M. tuberculosis) suggests M. gilvum may harbor unique adaptations.

Product Specs

Form
Lyophilized powder. We will ship the available format, but you can specify a format when ordering.
Lead Time
Delivery time varies by purchase method and location. Contact your local distributor for details. Proteins are shipped with blue ice packs by default; request dry ice in advance (extra fees 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. Reconstitute 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. Default glycerol concentration is 50%.
Shelf Life
Shelf life depends on storage conditions, buffer, temperature, and protein stability. Liquid form: 6 months at -20°C/-80°C. Lyophilized form: 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
Tag type is determined during manufacturing. If you require a specific tag, please inform us and we will prioritize its development.
Synonyms
atpD; Mflv_2318ATP 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
1-476
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Mycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK))
Target Names
atpD
Target Protein Sequence
MTSTEEKTTS GRVVRITGPV VDVEFPRGSV PELFNALHAD ITYKELSKTL TLEVAQHLGD NLVRTISMQP TDGLVRGVEV TDTGNSISVP VGDGVKGHVF NALGDCLDEP GYGKDFEHWS IHRKPPPFSE LEPRTEMLET GLKVVDLLTP YVRGGKIALF GGAGVGKTVL IQEMINRIAR NFGGTSVFAG VGERTREGND LWVELEDANV LKDTALVFGQ MDEPPGTRMR VALSALTMAE FFRDEQQQDV LLFIDNIFRF TQAGSEVSTL LGRMPSAVGY QPTLADEMGE LQERITSTRG RSITSMQAVY VPADDYTDPA PATTFAHLDA TTELSRTVFS KGIFPAVDPL ASSSTILDPA VVGDEHYRVA QEVIRILQRY KDLQDIIAIL GIDELAEEDK QLVQRARRLE RFLSQNMMAA EQFTGQPGST VPLKETIEAF DKLTKGEFDH LPEQAFFLIG GLDDLAKKAE SLGAKL
Uniprot No.

Target Background

Function
Generates ATP from ADP using a proton gradient. Catalytic sites are mainly within the beta subunits.
Database Links
Protein Families
ATPase alpha/beta chains family
Subcellular Location
Cell membrane; Peripheral membrane protein.

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