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protein_domains: NAD(P)-bd_dom_sf. (IPR036291); RCK_C. (IPR006037); RCK_C_sf. (IPR036721);
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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q72F06
• Protein Description: SubName: Full=Potassium uptake protein TrkA, putative {ECO:0000313|EMBL:AAS94895.1};
• Gene Information: OrderedLocusNames=DVU_0412 {ECO:0000313|EMBL:AAS94895.1};
• Organism (full): Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
• Protein Family: Not specified in UniProt
• Key Domains: NAD(P)-bd_dom_sf. (IPR036291); RCK_C. (IPR006037); RCK_C_sf. (IPR036721); RCK_N. (IPR003148); Trk_Ktr_HKT_K-transport. (IPR050721)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Q72F06" matches the protein description above
2. Verify the organism is correct: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'Q72F06' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene Q72F06 (gene ID: Q72F06, UniProt: Q72F06) in DESVH.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q72F06
• Protein Description: SubName: Full=Potassium uptake protein TrkA, putative {ECO:0000313|EMBL:AAS94895.1};
• Gene Information: OrderedLocusNames=DVU_0412 {ECO:0000313|EMBL:AAS94895.1};
• Organism (full): Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
• Protein Family: Not specified in UniProt
• Key Domains: NAD(P)-bd_dom_sf. (IPR036291); RCK_C. (IPR006037); RCK_C_sf. (IPR036721); RCK_N. (IPR003148); Trk_Ktr_HKT_K-transport. (IPR050721)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Q72F06" matches the protein description above
2. Verify the organism is correct: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'Q72F06' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene Q72F06 (gene ID: Q72F06, UniProt: Q72F06) in DESVH.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Plan overview
We verified the target and then assembled recent mechanistic and structural evidence about Trk/Ktr potassium uptake systems and their RCK (TrkA/KtrA/KtrC) regulatory subunits, prioritized 2023–2024 sources, and searched for organism-specific data for Desulfovibrio vulgaris Hildenborough (DVH). Evidence was synthesized into a functional annotation for DVU_0412 (UniProt Q72F06), with explicit notes where organism-specific literature is lacking.

Protein identity verification and domain context
• Identity: The query protein is UniProt Q72F06, annotated as a TrkA-like potassium uptake protein (ordered locus DVU_0412) from Nitratidesulfovibrio (Desulfovibrio) vulgaris Hildenborough. The UniProt description explicitly matches a cytosolic TrkA/RCK-type regulator for a Trk/Ktr K+ uptake system (user-provided record).
• Organism: Nitratidesulfovibrio vulgaris (strain Hildenborough) as provided; no conflicting symbols or aliases were found in the literature screened here.
• Domains/family: The provided domain architecture (NAD(P)-binding-like superfamily; RCK_N and RCK_C; Trk/Ktr/HKT K-transport association) is consistent with the canonical RCK (regulator of K+ conductance) domains that form gating “rings” for bacterial Trk/Ktr systems (reviewed in 2024) (foster2024bacterialcellvolume pages 6-8).

Key concepts and definitions (current understanding)
• Trk/Ktr K+ uptake systems: Heteromeric bacterial K+ importers that combine a cytosolic RCK regulatory subunit (TrkA/KtrA/KtrC) and a membrane pore-forming subunit (TrkH/KtrB/KtrD). These systems act as ATP-gated channels with activity tuned by cellular signals, notably the second messenger c-di-AMP, and by ions such as Na+ (review) (foster2024bacterialcellvolume pages 6-8). Architecturally, the RCK subunits form an octameric gating ring that docks to the dimeric membrane pore to control K+ flux (cryo-EM/structural) (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9).
• RCK regulation and nucleotide gating: ATP binding to the RCK ring activates, whereas ADP-bound conformations are inactive/closed; conformational changes in the RCK ring are transmitted to gate residues in the membrane subunit (e.g., Arg417 and Phe91 in BsKtrB) (2024 cryo-EM) (chiang2024structuralbasisand pages 8-9, chiang2024structuralbasisand pages 1-2).
• Na+-dependent activation: Recent cryo-EM and biophysical work demonstrated a Na+ binding site at the intra-dimer interface of ATP-bound KtrA (Bacillus subtilis). Na+ binding stabilizes the ATP-bound state and synergistically enhances K+ flux through KtrAB (2024) (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9).
• c-di-AMP signaling: c-di-AMP is a master regulator of bacterial cell volume and K+ homeostasis. It often binds RCK-family subunits (TrkA/KtrA/KtrC) and other K+ transport components, tuning transport and osmoadaptation (2024 review) (foster2024bacterialcellvolume pages 6-8). Organismal studies show that elevated c-di-AMP generally reduces K+ import capacity, while reduced c-di-AMP risks toxic K+ accumulation (foster2024bacterialcellvolume pages 6-8).

Recent developments and latest research (2023–2024 priority)
• Synergistic ATP/Na+ activation of KtrAB: High-resolution structures of B. subtilis KtrAB solved in ATP- and ADP-bound states identify a Na+ site in the ATP-bound RCK ring and delineate pore gating residues (Arg417, Phe91). Functional assays show Na+ stabilizes the ATP-bound complex and increases K+ flux (Nature Communications, May 2024; https://doi.org/10.1038/s41467-024-48057-y) (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9).
• c-di-AMP control of K+ import and virulence outputs: In Bacillus anthracis, c-di-AMP accumulation down-regulates K+ importers through both protein (KdpD) and riboswitch (ydaO) mechanisms, reducing anthrax toxin expression; manipulating Ktr/Kdp components modulates intracellular K+ and rescues phenotypes (Microbiology Spectrum, Aug 2024; https://doi.org/10.1128/spectrum.03786-23) (hu2024cdiampaccumulationimpairs pages 6-9).
• Broader RCK architecture and ligand binding: Structural work on the RCK-bearing K+/H+ exchanger KefC highlights conserved RCK/KTN folds and nucleotide/ligand binding that modulate coupling between cytosolic RCKs and membrane transport modules, underscoring generalizable principles for TrkA-like proteins (Nature Communications, Jun 2024; https://doi.org/10.1038/s41467-024-49082-7) (gulati2024structureandmechanism pages 6-8).
• State-of-the-art synthesis: An authoritative 2024 review quantitatively frames c-di-AMP as a master regulator of K+ transport systems (Trk/Ktr/Kup/Kdp), consolidating genetic and structural evidence that RCK subunits are central c-di-AMP receptors across many bacteria (MMBR, Jun 2024; https://doi.org/10.1128/mmbr.00181-23) (foster2024bacterialcellvolume pages 6-8).

Current applications and real-world implementations
• Stress adaptation and growth: KtrA-associated systems are important for survival under osmotic and pH stresses; deletion of KtrA homologs impairs growth in low K+ and saline/alkaline conditions, effects which can be rescued by K+ supplementation or complementation, demonstrating practical roles in environmental resilience (Frontiers in Microbiology, Feb 2023; https://doi.org/10.3389/fmicb.2023.1117684) (acciarri2023redundantpotassiumtransporter pages 8-10).
• Pathogenesis leverage points: Modulating K+ uptake via c-di-AMP signaling affects virulence determinant expression (e.g., B. anthracis toxin), offering translational angles for antimicrobial strategies that perturb c-di-AMP–K+ transport networks (Microbiology Spectrum, Aug 2024; https://doi.org/10.1128/spectrum.03786-23) (hu2024cdiampaccumulationimpairs pages 6-9).

Expert opinions and analysis from authoritative sources
• Foster et al. (2024, MMBR) conclude that c-di-AMP is a master regulator of cell volume with most molecular targets linked to K+ and osmolyte homeostasis; they emphasize that TrkA/KtrA/KtrC RCK subunits are key c-di-AMP receptors and that transporter redundancy underpins robustness of K+ homeostasis (https://doi.org/10.1128/mmbr.00181-23) (foster2024bacterialcellvolume pages 6-8).
• Chiang et al. (2024, Nat Comm) resolve the mechanistic basis for ATP/ADP gating and reveal a Na+-binding site in the ATP-bound RCK ring, establishing synergy between ATP and Na+ in activating KtrAB (https://doi.org/10.1038/s41467-024-48057-y) (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9).
• Gulati et al. (2024, Nat Comm) provide structural principles of RCK/KTN domains and their ligand interactions that are shared across K+ transport systems, reinforcing the conserved regulatory logic applicable to TrkA-like proteins (https://doi.org/10.1038/s41467-024-49082-7) (gulati2024structureandmechanism pages 6-8).
• Organismal-level evidence supports redundancy and compensatory regulation among Ktr/Kup/Kdp systems under stress, highlighting the physiological indispensability of RCK-controlled K+ uptake (Frontiers in Microbiology, 2023; https://doi.org/10.3389/fmicb.2023.1117684) (acciarri2023redundantpotassiumtransporter pages 8-10).

Relevant statistics and recent data
• Affinity/regulation: RCK-family subunits across bacteria bind c-di-AMP with KD values reported in the ~40 nM–8 µM range (range summarized in 2024 review) (foster2024bacterialcellvolume pages 6-8).
• System properties: Trk/Ktr systems are typically low-affinity (KM around 1 mM) K+ importers that function effectively when external K+ is not limiting, using membrane potential and ATP-gating by RCK rings (foster2024bacterialcellvolume pages 6-8).
• Redundancy patterns: In Enterococcus, Ktr (KtrA/KtrB) is broadly present across analyzed species, whereas Trk is rarer, and Kdp pumps occur only in a minority of strains, indicating networked redundancy with Ktr and Kup/KimA transporters predominating (acciarri2023redundantpotassiumtransporter pages 8-10). In B. anthracis, c-di-AMP accumulation reduces ktr and kdp transcripts by ~2–5-fold and manipulating either system modulates intracellular K+ by up to ~4-fold, illustrating cross-regulation and functional redundancy (hu2024cdiampaccumulationimpairs pages 6-9).

Organism-specific assessment for DVU_0412 (Q72F06) in Desulfovibrio vulgaris Hildenborough
• Ambiguity check: No conflicting gene/protein symbol usage was found for DVU_0412 in our search; “Q72F06” is a UniProt accession, not a symbol, minimizing ambiguity.
• Literature availability: We did not find primary, organism-specific experimental studies on DVU_0412 or a D. vulgaris Hildenborough Trk/Ktr operon in the 2023–2024 literature sampled here. Therefore, direct organism-level functional evidence for DVU_0412 remains limited in the recent record screened.
• Inference from conserved domains and system biology: Given the RCK_N/RCK_C domains and Trk/Ktr association in the UniProt entry, and the conserved architecture across bacteria, DVU_0412 most likely encodes a cytosolic RCK gating subunit (TrkA-like) that forms an octameric ring and associates with a cognate TrkH/KtrB-like membrane pore to mediate K+ uptake. Its activity is expected to be ATP/ADP-gated, further activated by Na+ (as shown for KtrAB), and down-modulated by c-di-AMP binding to the RCK subunit, consistent with the conserved regulatory paradigm (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9, foster2024bacterialcellvolume pages 6-8, hu2024cdiampaccumulationimpairs pages 6-9, gulati2024structureandmechanism pages 6-8).
• Predicted cellular localization and complex: Cytosolic protein assembling as an RCK ring that docks to an inner-membrane KtrB/TrkH channel; thus, DVU_0412’s functional site would be the cytosol–inner membrane interface of DVH cells (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9, foster2024bacterialcellvolume pages 6-8).
• Pathway context: Potassium homeostasis and osmoadaptation. Likely interplay with other K+ systems (e.g., Kup/KimA-like symporters or Kdp-type pumps if present) under varying salinity/pH conditions, following patterns seen in other bacteria (acciarri2023redundantpotassiumtransporter pages 8-10, hu2024cdiampaccumulationimpairs pages 6-9, foster2024bacterialcellvolume pages 6-8).

Mechanistic model for DVU_0412 function (evidence-based)
• Primary function: Cytosolic RCK regulator (TrkA-like) for a Trk/Ktr K+ uptake complex. Substrate of the overall system: K+; DVU_0412 itself is not the pore but the ligand-gated regulator controlling K+ flux through the membrane partner (foster2024bacterialcellvolume pages 6-8, chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9).
• Ligand regulation: ATP binding to DVU_0412’s RCK domains promotes an active, open-channel state in the associated membrane pore; ADP stabilizes a closed/inactive conformation. Na+ binding to the ATP-bound RCK ring further stabilizes the active conformation, enhancing flux (2024 structural-functional data) (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9).
• Second-messenger control: c-di-AMP is expected to bind the RCK subunit (or other K+ transport components) and reduce K+ uptake capacity, tuning intracellular K+ and osmotic balance, as broadly demonstrated in multiple bacteria (MMBR 2024 review and organismal studies) (foster2024bacterialcellvolume pages 6-8, hu2024cdiampaccumulationimpairs pages 6-9).
• Localization: Cytosolic oligomeric ring apposed to the inner membrane, docking to a TrkH/KtrB pore (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9).

Concise evidence table
| Source (author, year) | Topic / Focus | Key Finding relevant to TrkA/KtrA/RCK and K+ uptake | Organism | URL / DOI | Relevance to Q72F06 (DVU_0412) | Notes on methods |
|---|---|---|---|---|---|---|
| Foster 2024 | Review: c-di-AMP and cell volume / K+ homeostasis | c-di-AMP is a central regulator of bacterial K+ transport; RCK-family soluble subunits (TrkA/KtrA/KtrC) form cytosolic rings that gate membrane K+ pores and are modulated by nucleotide and c-di-AMP levels, altering K+ import activity (high c-di-AMP → reduced import). (foster2024bacterialcellvolume pages 6-8) | Broad (Firmicutes/Actinobacteria examples; Bacillus) | https://doi.org/10.1128/mmbr.00181-23 | Indirect — provides authoritative mechanistic framework supporting TrkA annotation | Review synthesizing biochemical, genetic, structural studies |
| Acciarri 2023 | Redundancy of K+ transporters under stress | Multiple K+ uptake systems (Ktr, Kup, Kdp, KimA) provide functional redundancy; loss of KtrA impairs growth under stress, illustrating physiological importance of RCK-associated channels for survival. (acciarri2023redundantpotassiumtransporter pages 12-12) | Enterococcus faecalis | https://doi.org/10.3389/fmicb.2023.1117684 | Indirect — supports prevalence and physiological role of KtrA-like proteins in bacteria | Genetic knockouts, growth assays, comparative genomics |
| Vevik 2025 | Experimental characterization of TrkA homolog | A TrkA homologue binds c-di-AMP with high affinity, forms octameric RCK assemblies, and is required for growth in low-K+ conditions, directly linking TrkA function to c-di-AMP regulation of K+ uptake. (vevik2025trkaofstreptococcus pages 1-2) | Streptococcus mitis | https://doi.org/10.1099/mic.0.001597 | Indirect (organism different) — strong functional evidence that TrkA-type proteins act as c-di-AMP-responsive gating subunits | Gene deletion, recombinant expression, SEC oligomerization, in vitro ligand binding |
| Stautz 2025 | Structural mechanism of KtrAB regulation (RCK–pore interface) | Cryo-EM and MD reveal ATP/ADP-dependent conformational changes in RCK rings that allosterically gate KtrB pores; identify N-terminal IDRs in KtrB important for transmitting RCK signals and note Na+/nucleotide synergism in activation. (stautz2025ashortintrinsically pages 13-14) | Vibrio alginolyticus (structural/comparative analyses) | https://doi.org/10.1038/s41467-025-59546-z | Indirect — provides structural template and gating mechanism applicable to TrkA-like proteins such as Q72F06 | Cryo-EM, molecular dynamics, functional assays |

Table: Compact table summarizing key literature supporting functional annotation of Q72F06 (DVU_0412) as a TrkA-like RCK regulatory subunit for bacterial K+ uptake; citations point to mechanistic, physiological, and structural evidence useful for inferring function in Desulfovibrio vulgaris.

Gaps and recommendations
• Organism-specific confirmation: No 2023–2024 experimental reports for DVU_0412 or a DVH Trk/Ktr operon were located here. We recommend targeted genomic context analysis (operon neighborhood for DVU_0412), expression under K+-limitation/salt stress, and biochemical tests of c-di-AMP binding to DVU_0412, guided by assays used in recent TrkA studies (e.g., binding assays and SEC oligomerization seen in S. mitis) (vevik2025trkaofstreptococcus pages 2-4, vevik2025trkaofstreptococcus pages 1-2).

Summary functional annotation for Q72F06 (DVU_0412)
• Likely role: Cytosolic TrkA-like RCK regulatory subunit that gates a Trk/Ktr K+ uptake channel in DVH, contributing to potassium homeostasis and osmoadaptation (foster2024bacterialcellvolume pages 6-8, chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9).
• Regulation: Activated by ATP and further stabilized by Na+; inactivated by ADP. Expected negative regulation by c-di-AMP binding, in line with conserved mechanisms (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9, foster2024bacterialcellvolume pages 6-8, hu2024cdiampaccumulationimpairs pages 6-9).
• Localization/complex: Cytosolic oligomer (RCK ring) docking to an inner membrane TrkH/KtrB-type pore (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9).
• Pathway: Potassium uptake and cell volume control; functionally redundant with other K+ systems typical of bacteria, enabling stress resilience (acciarri2023redundantpotassiumtransporter pages 8-10, foster2024bacterialcellvolume pages 6-8, hu2024cdiampaccumulationimpairs pages 6-9).

Citations with URLs and dates
• Chiang WT et al. Structural basis and synergism of ATP and Na+ activation in bacterial K+ uptake system KtrAB. Nature Communications. May 2024. doi:10.1038/s41467-024-48057-y. https://doi.org/10.1038/s41467-024-48057-y (chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9)
• Foster AJ, van den Noort M, Poolman B. Bacterial cell volume regulation and the importance of cyclic di-AMP. Microbiol Mol Biol Rev. Jun 2024. doi:10.1128/mmbr.00181-23. https://doi.org/10.1128/mmbr.00181-23 (foster2024bacterialcellvolume pages 6-8)
• Hu J et al. c-di-AMP accumulation impairs toxin expression of Bacillus anthracis by down-regulating potassium importers. Microbiology Spectrum. Aug 2024. doi:10.1128/spectrum.03786-23. https://doi.org/10.1128/spectrum.03786-23 (hu2024cdiampaccumulationimpairs pages 6-9)
• Gulati A et al. Structure and mechanism of the K+/H+ exchanger KefC. Nature Communications. Jun 2024. doi:10.1038/s41467-024-49082-7. https://doi.org/10.1038/s41467-024-49082-7 (gulati2024structureandmechanism pages 6-8)
• Acciarri G et al. Redundant potassium transporter systems guarantee the survival of Enterococcus faecalis under stress conditions. Frontiers in Microbiology. Feb 2023. doi:10.3389/fmicb.2023.1117684. https://doi.org/10.3389/fmicb.2023.1117684 (acciarri2023redundantpotassiumtransporter pages 8-10)
• Vevik K et al. TrkA of Streptococcus mitis binds c-di-AMP and is required for growth in low potassium conditions. Microbiology. Aug 2025. doi:10.1099/mic.0.001597. https://doi.org/10.1099/mic.0.001597 (used to illustrate conserved TrkA properties; not prioritized for 2023–2024 but supportive) (vevik2025trkaofstreptococcus pages 1-2, vevik2025trkaofstreptococcus pages 6-9, vevik2025trkaofstreptococcus pages 2-4)

Limitations
• The gene symbol “Q72F06” is a UniProt accession, minimizing symbol ambiguity; however, organism-specific experimental literature for DVU_0412 in DVH is limited in the recent timeframe. The functional annotation above is therefore primarily inferred from conserved domain architecture and recent mechanistic work on bacterial Trk/Ktr systems (foster2024bacterialcellvolume pages 6-8, chiang2024structuralbasisand pages 1-2, chiang2024structuralbasisand pages 8-9, hu2024cdiampaccumulationimpairs pages 6-9).

References

1. (foster2024bacterialcellvolume pages 6-8): Alexander J. Foster, Marco van den Noort, and Bert Poolman. Bacterial cell volume regulation and the importance of cyclic di-amp. Microbiology and Molecular Biology Reviews, Jun 2024. URL: https://doi.org/10.1128/mmbr.00181-23, doi:10.1128/mmbr.00181-23. This article has 16 citations and is from a domain leading peer-reviewed journal.

2. (chiang2024structuralbasisand pages 1-2): Wesley Tien Chiang, Yao-Kai Chang, Wei-Han Hui, Shu-Wei Chang, Chen-Yi Liao, Yi-Chuan Chang, Chun-Jung Chen, Wei-Chen Wang, Chien-Chen Lai, Chun-Hsiung Wang, Siou-Ying Luo, Ya-Ping Huang, Shan-Ho Chou, Tzyy-Leng Horng, Ming-Hon Hou, Stephen P. Muench, Ren-Shiang Chen, Ming-Daw Tsai, and Nien-Jen Hu. Structural basis and synergism of atp and na+ activation in bacterial k+ uptake system ktrab. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48057-y, doi:10.1038/s41467-024-48057-y. This article has 5 citations and is from a highest quality peer-reviewed journal.

3. (chiang2024structuralbasisand pages 8-9): Wesley Tien Chiang, Yao-Kai Chang, Wei-Han Hui, Shu-Wei Chang, Chen-Yi Liao, Yi-Chuan Chang, Chun-Jung Chen, Wei-Chen Wang, Chien-Chen Lai, Chun-Hsiung Wang, Siou-Ying Luo, Ya-Ping Huang, Shan-Ho Chou, Tzyy-Leng Horng, Ming-Hon Hou, Stephen P. Muench, Ren-Shiang Chen, Ming-Daw Tsai, and Nien-Jen Hu. Structural basis and synergism of atp and na+ activation in bacterial k+ uptake system ktrab. Nature Communications, May 2024. URL: https://doi.org/10.1038/s41467-024-48057-y, doi:10.1038/s41467-024-48057-y. This article has 5 citations and is from a highest quality peer-reviewed journal.

4. (hu2024cdiampaccumulationimpairs pages 6-9): Jia Hu, Junmin Yao, Chengfeng Lei, and Xiulian Sun. C-di-amp accumulation impairs toxin expression of bacillus anthracis by down-regulating potassium importers. Microbiology Spectrum, Aug 2024. URL: https://doi.org/10.1128/spectrum.03786-23, doi:10.1128/spectrum.03786-23. This article has 3 citations and is from a domain leading peer-reviewed journal.

5. (gulati2024structureandmechanism pages 6-8): Ashutosh Gulati, Surabhi Kokane, Annemarie Perez-Boerema, Claudia Alleva, Pascal F. Meier, Rei Matsuoka, and David Drew. Structure and mechanism of the k+/h+ exchanger kefc. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-49082-7, doi:10.1038/s41467-024-49082-7. This article has 10 citations and is from a highest quality peer-reviewed journal.

6. (acciarri2023redundantpotassiumtransporter pages 8-10): Giuliana Acciarri, Fernán O. Gizzi, Mariano A. Torres Manno, Jörg Stülke, Martín Espariz, Víctor S. Blancato, and Christian Magni. Redundant potassium transporter systems guarantee the survival of enterococcus faecalis under stress conditions. Frontiers in Microbiology, Feb 2023. URL: https://doi.org/10.3389/fmicb.2023.1117684, doi:10.3389/fmicb.2023.1117684. This article has 13 citations and is from a poor quality or predatory journal.

7. (acciarri2023redundantpotassiumtransporter pages 12-12): Giuliana Acciarri, Fernán O. Gizzi, Mariano A. Torres Manno, Jörg Stülke, Martín Espariz, Víctor S. Blancato, and Christian Magni. Redundant potassium transporter systems guarantee the survival of enterococcus faecalis under stress conditions. Frontiers in Microbiology, Feb 2023. URL: https://doi.org/10.3389/fmicb.2023.1117684, doi:10.3389/fmicb.2023.1117684. This article has 13 citations and is from a poor quality or predatory journal.

8. (vevik2025trkaofstreptococcus pages 1-2): Kristina Vevik, Biramitha Sribasgaran, Kun Cai, Ali-Oddin Naemi, Håkon Pedersen Kaspersen, Silvio Uhlig, O. Økstad, and Roger Simm. Trka of streptococcus mitis ccug31611 binds cyclic di-adenosine monophosphate and is required for growth in low potassium conditions. Microbiology, Aug 2025. URL: https://doi.org/10.1099/mic.0.001597, doi:10.1099/mic.0.001597. This article has 0 citations and is from a peer-reviewed journal.

9. (stautz2025ashortintrinsically pages 13-14): Janina Stautz, David Griwatz, Susann Kaltwasser, Ahmad Reza Mehdipour, Sophie Ketter, Celina Thiel, Dorith Wunnicke, Marina Schrecker, Deryck J. Mills, Gerhard Hummer, Janet Vonck, and Inga Hänelt. A short intrinsically disordered region at ktrb’s n-terminus facilitates allosteric regulation of k+ channel ktrab. Nature Communications, May 2025. URL: https://doi.org/10.1038/s41467-025-59546-z, doi:10.1038/s41467-025-59546-z. This article has 0 citations and is from a highest quality peer-reviewed journal.

10. (vevik2025trkaofstreptococcus pages 2-4): Kristina Vevik, Biramitha Sribasgaran, Kun Cai, Ali-Oddin Naemi, Håkon Pedersen Kaspersen, Silvio Uhlig, O. Økstad, and Roger Simm. Trka of streptococcus mitis ccug31611 binds cyclic di-adenosine monophosphate and is required for growth in low potassium conditions. Microbiology, Aug 2025. URL: https://doi.org/10.1099/mic.0.001597, doi:10.1099/mic.0.001597. This article has 0 citations and is from a peer-reviewed journal.

11. (vevik2025trkaofstreptococcus pages 6-9): Kristina Vevik, Biramitha Sribasgaran, Kun Cai, Ali-Oddin Naemi, Håkon Pedersen Kaspersen, Silvio Uhlig, O. Økstad, and Roger Simm. Trka of streptococcus mitis ccug31611 binds cyclic di-adenosine monophosphate and is required for growth in low potassium conditions. Microbiology, Aug 2025. URL: https://doi.org/10.1099/mic.0.001597, doi:10.1099/mic.0.001597. This article has 0 citations and is from a peer-reviewed journal.

Citations

1. foster2024bacterialcellvolume pages 6-8
2. hu2024cdiampaccumulationimpairs pages 6-9
3. gulati2024structureandmechanism pages 6-8
4. acciarri2023redundantpotassiumtransporter pages 8-10
5. acciarri2023redundantpotassiumtransporter pages 12-12
6. vevik2025trkaofstreptococcus pages 1-2
7. stautz2025ashortintrinsically pages 13-14
8. chiang2024structuralbasisand pages 1-2
9. chiang2024structuralbasisand pages 8-9
10. vevik2025trkaofstreptococcus pages 2-4
11. vevik2025trkaofstreptococcus pages 6-9
12. https://doi.org/10.1038/s41467-024-48057-y
13. https://doi.org/10.1128/spectrum.03786-23
14. https://doi.org/10.1038/s41467-024-49082-7
15. https://doi.org/10.1128/mmbr.00181-23
16. https://doi.org/10.3389/fmicb.2023.1117684
17. https://doi.org/10.1099/mic.0.001597
18. https://doi.org/10.1038/s41467-025-59546-z
19. https://doi.org/10.1128/mmbr.00181-23,
20. https://doi.org/10.1038/s41467-024-48057-y,
21. https://doi.org/10.1128/spectrum.03786-23,
22. https://doi.org/10.1038/s41467-024-49082-7,
23. https://doi.org/10.3389/fmicb.2023.1117684,
24. https://doi.org/10.1099/mic.0.001597,
25. https://doi.org/10.1038/s41467-025-59546-z,