Commercial preparations of Recombinant Shewanella woodyi UbiB undergo rigorous quality control measures to ensure consistent performance in research applications. While specific purity data for S. woodyi UbiB is not provided in the search results, similar recombinant proteins from related Shewanella species typically achieve purity levels greater than 90% as determined by SDS-PAGE analysis . This high purity standard ensures minimal interference from contaminants in downstream applications such as enzymatic assays, structural studies, or antibody production.
Based on comparative analysis with homologous proteins from related Shewanella species, UbiB from S. woodyi is classified as a probable protein kinase involved in ubiquinone biosynthesis. Similar proteins in the Shewanella genus, such as UbiB from Shewanella baltica, are categorized under EC 2.7.-.- (Transferring phosphorus-containing groups), indicating their role in phosphorylation reactions . The enzymatic function of UbiB is intimately linked to the regulation of ubiquinone synthesis, a critical process in aerobic energy metabolism.
The protein likely acts as a regulatory kinase that modulates the activity of other enzymes in the ubiquinone biosynthetic pathway. Specifically, evidence from related bacterial systems suggests that UbiB may regulate UbiI activity, an essential hydroxylase in the ubiquinone biosynthesis pathway . This regulatory function ensures proper coordination of the multiple enzymatic steps required for ubiquinone production under varying environmental conditions.
Ubiquinone (Coenzyme Q) is an essential lipid-soluble electron carrier in the respiratory chain of bacteria. The biosynthesis of this critical molecule involves a complex pathway with multiple enzymatic steps. UbiB plays a crucial regulatory role in this pathway, potentially through phosphorylation of key enzymes or intermediates. The protein's structure, featuring both kinase domains and membrane-associated regions, allows it to integrate metabolic signals and coordinate ubiquinone production according to cellular energy demands.
In Shewanella woodyi, a bioluminescent marine bacterium, efficient energy metabolism is particularly important for supporting both growth and light production. The UbiB protein's regulatory function in ubiquinone biosynthesis therefore has implications not only for general cellular respiration but potentially also for the specific energy requirements of bioluminescence, a distinctive characteristic of this bacterial species .
Comparing the UbiB protein from Shewanella woodyi with its homologs from other Shewanella species reveals significant evolutionary conservation, reflecting the critical nature of this protein in bacterial metabolism. The UbiB protein from Shewanella amazonensis, for instance, also consists of 549 amino acids, matching the length of S. woodyi UbiB . This conservation in protein size suggests preservation of fundamental structural elements required for function.
Recombinant Shewanella woodyi UbiB protein serves as a valuable research tool for investigating various aspects of bacterial metabolism and physiology. Specific applications include:
Structural studies to elucidate the three-dimensional configuration of the protein and its functional domains
Enzymatic assays to characterize the kinase activity and substrate specificity
Protein-protein interaction studies to identify binding partners within the ubiquinone biosynthesis pathway
Comparative biochemical analyses across different bacterial species to understand evolutionary adaptations
The availability of high-purity recombinant protein facilitates these investigations, enabling researchers to gain deeper insights into fundamental aspects of bacterial energy metabolism and its regulation.
Shewanella woodyi is a bioluminescent marine bacterium, and research has shown that even within this species, different strains exhibit diverse characteristics including variations in growth patterns, enzymatic activities, carbon source utilization, and antibiotic resistance profiles . The genetic diversity among S. woodyi strains has been demonstrated through techniques such as pulsed-field gel electrophoresis (PFGE), which revealed restriction fragment pattern homology ranging from 56 to 89% with SmaI enzyme and 82 to 94% with NotI enzyme .
Understanding the role of UbiB in such organisms provides insights into the energy requirements and metabolic pathways supporting bioluminescence. The protein's involvement in ubiquinone biosynthesis directly impacts the electron transport chain efficiency, which in turn affects the energy available for light production. This connection makes UbiB an interesting target for studies aimed at understanding the metabolic underpinnings of bacterial bioluminescence.
This protein is likely a protein kinase regulator of UbiI activity, which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
KEGG: swd:Swoo_0525
STRING: 392500.Swoo_0525