Recombinant Yersinia pestis bv. Antiqua Succinyl-CoA ligase [ADP-forming] subunit beta (sucC)

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Description

Overview of Succinyl-CoA Ligase [ADP-Forming] Subunit Beta (SucC) in Yersinia pestis bv. Antiqua

Succinyl-CoA ligase [ADP-forming] subunit beta (SucC) is a mitochondrial metabolic enzyme that catalyzes the reversible conversion of succinyl-CoA to succinate in the tricarboxylic acid (TCA) cycle, coupled with ATP/ADP phosphorylation. In Yersinia pestis biovar Antiqua, this enzyme is encoded by the sucC gene (annotated as sucB in some bacterial systems). While its canonical role involves energy production, recent studies suggest non-metabolic functions in stress response and pathogen adaptation .

Non-Canonical Roles in Pathogenesis

While sucC is primarily metabolic, studies in human homologs (SUCLA2) reveal redox regulation via stress granule assembly during cellular stress . Although direct evidence in Y. pestis is limited, analogous mechanisms may exist:

  • Oxidative Stress Mitigation: SUCLA2 in humans enhances catalase translation to combat reactive oxygen species (ROS) .

  • Anoikis Resistance: Mitochondrial-to-cytosolic translocation of SUCLA2 promotes cancer cell survival during detachment .

These findings imply that Y. pestis SucC could similarly support bacterial survival under host-induced stress (e.g., phagocytosis), though experimental validation is needed .

Comparative Genomics of Y. pestis Biovar Antiqua

Analysis of Antiqua genomes reveals strain-specific adaptations:

Table 1: Shared Gene Losses in Y. pestis Biovar Antiqua vs. Other Strains49

Function LostAntiquaCO92KIM
TccC-family insecticidal toxinYesNoYes
Ail-like adhesinPartialNoYes
RTX toxin transporterNoYesYes

Antiqua retains metabolic genes like sucC but shows lineage-specific pseudogenization in virulence-associated loci (e.g., ail, yop effectors) .

Recombinant Applications and Research Gaps

  • Functional Characterization: No structural or enzymatic studies on purified SucC from Antiqua.

  • Metabolic vs. Virulence Roles: Unclear if sucC deletion impacts Y. pestis survival in hosts.

Future Directions

  1. Structural Studies: Resolve SucC’s crystal structure to identify ATP/CoA-binding sites.

  2. Gene Knockout Models: Assess ΔsucC strains for metabolic and virulence defects.

  3. Stress Response Assays: Test SucC’s role under oxidative or nutrient-limited conditions.

Product Specs

Form
Lyophilized powder. We will ship the format we have in stock. If you have special format requirements, please note them when ordering.
Lead Time
Delivery time varies by purchase method and location. Consult local distributors for specific delivery times. Proteins are shipped with blue ice packs by default. For dry ice shipment, contact us 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 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, 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
sucC; YpAngola_A1386; Succinate--CoA ligase [ADP-forming] subunit beta; EC 6.2.1.5; Succinyl-CoA synthetase subunit beta; SCS-beta
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-388
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Yersinia pestis bv. Antiqua (strain Angola)
Target Names
sucC
Target Protein Sequence
MNLHEYQAKQ LFARYGMPAP TGYACTTPRE AEEAASKIGA GPWVVKCQVH AGGRGKAGGV KLVNSKEDIR AFAEQWLGKK LVTYQTDANG QPVHQILVEA ATDIDKELYL GAVIDRSSRR VVFMASTEGG VEIEKVAEET PELIHKIALD PLTGPQPYQG RELAFKLGLT GKQVGQFTKI FMGLATLFLE RDLAMVEINP LVVTKQGDLI CLDGKLGADG NALFRQPELR EMRDPSQEDA REAHAAQWEL NYVALDGNIG CMVNGAGLAM GTMDIVKLHG GEPANFLDVG GGATKERVTE AFKIILSDDK VKAVFVNIFG GIVRCDLIAD GIIGAVEEVG VNVPVVVRLE GNNAELGAKK LADSGLNIIA ATSLTDAAQQ VVAAVGAK
Uniprot No.

Target Background

Function
Succinyl-CoA synthetase is involved in the citric acid cycle (TCA). It couples succinyl-CoA hydrolysis to ATP or GTP synthesis, representing the only substrate-level phosphorylation step in the TCA. The beta subunit determines nucleotide specificity and binds succinate. The alpha subunit binds coenzyme A and phosphate.
Database Links
Protein Families
Succinate/malate CoA ligase beta subunit family

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