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gene_id: Q72FD5
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gene_info: OrderedLocusNames=DVU_0279 {ECO:0000313|EMBL:AAS94762.1};
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
protein_domains: SLC26A/SulP_dom. (IPR011547); SLC26A/SulP_fam. (IPR001902); STAS_dom.
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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: Q72FD5
• Protein Description: SubName: Full=Sulfate permease family protein {ECO:0000313|EMBL:AAS94762.1};
• Gene Information: OrderedLocusNames=DVU_0279 {ECO:0000313|EMBL:AAS94762.1};
• 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: SLC26A/SulP_dom. (IPR011547); SLC26A/SulP_fam. (IPR001902); STAS_dom. (IPR002645); STAS_dom_sf. (IPR036513); STAS (PF01740)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Q72FD5" 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 'Q72FD5' 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 Q72FD5 (gene ID: Q72FD5, UniProt: Q72FD5) 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: Q72FD5
• Protein Description: SubName: Full=Sulfate permease family protein {ECO:0000313|EMBL:AAS94762.1};
• Gene Information: OrderedLocusNames=DVU_0279 {ECO:0000313|EMBL:AAS94762.1};
• 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: SLC26A/SulP_dom. (IPR011547); SLC26A/SulP_fam. (IPR001902); STAS_dom. (IPR002645); STAS_dom_sf. (IPR036513); STAS (PF01740)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Q72FD5" 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 'Q72FD5' 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 Q72FD5 (gene ID: Q72FD5, UniProt: Q72FD5) 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.

Research plan and verification
- Identity check: UniProt Q72FD5 corresponds to DVU_0279 from Desulfovibrio vulgaris subsp. vulgaris Hildenborough (ATCC 29579/DSM 644). It is annotated as a Sulfate permease family (SulP/SLC26) protein containing a cytosolic STAS domain. The domain architecture aligns with SLC26/SulP transporters (SLC26A/SulP core plus STAS) (marietou2018sulfatetransportersin pages 1-2, marietou2018sulfatetransportersin pages 20-20).
- Organism specificity: Comparative genomics explicitly identifies DVU0279 as one of three SulP-type transporters in D. vulgaris Hildenborough alongside DVU0053 and DVU1999 (marietou2018sulfatetransportersin pages 16-17).

1) Key concepts and definitions with current understanding
- SulP/SLC26 transporters: A widely distributed family of secondary-active anion transporters that move inorganic anions (e.g., sulfate, bicarbonate, chloride, oxalate, iodide in some members) across membranes. They often include a C-terminal STAS (Sulfate Transporter and Anti-Sigma factor antagonist) domain involved in regulation and biogenesis (wang2024mechanismofanion pages 1-2, marietou2018sulfatetransportersin pages 20-20). Mechanistically, SLC26 family transporters operate via elevator-type alternating access, with recent structures showing multiple anion-binding sites (wang2024mechanismofanion pages 1-2).
- STAS domain: The cytosolic STAS domain of SLC26/SulP proteins modulates transporter function and biogenesis; recent structural-functional work demonstrates direct interactions between STAS and transmembrane regions that influence anion selectivity and exchange (wang2024mechanismofanion pages 1-2). Earlier work in plants and bacteria also implicated STAS in transporter maturation and regulation (marietou2018sulfatetransportersin pages 20-20).
- Sulfate uptake in sulfate-reducing microorganisms (SRM): The first step of dissimilatory sulfate reduction is import of sulfate, which strongly affects reduction rates. Multiple transporter families can mediate uptake in SRM, especially SulP and CysZ; ABC-type SulT is generally not implicated in SRM sulfate uptake (marietou2018sulfatetransportersin pages 1-2, marietou2018sulfatetransportersin pages 3-4, marietou2018sulfatetransportersin pages 2-3).

2) Recent developments and latest research (priority 2023–2024)
- Mechanism of SLC26 anion exchange and STAS regulation: Cryo-EM structures of pendrin (SLC26A4) resolved two anion-binding sites per protomer and revealed direct STAS–transmembrane interactions that modulate anion exchange and selectivity; the inhibitor niflumic acid was shown to compete with anion binding and impede conformational transitions (wang2024mechanismofanion pages 1-2). These results underpin a general mechanistic framework applicable to bacterial SulP homologs like DVU_0279.
- Broader family behavior (context beyond 2024): SLC26A11 has been described as a dual-function lysosomal sulfate transporter and uncoupled chloride conductance, consistent with elevator-type mechanism and proton:sulfate coupling (kuhn2025slc26a11isan pages 1-4). While outside the 2023–2024 window and in mammals, it reinforces mechanistic principles for the family.

3) Current applications and real-world implementations
- Structural mechanism informs inhibitor design: The 2024 pendrin study identified binding sites and inhibition by niflumic acid, illustrating how structure-guided modulation of SLC26 transport is feasible (wang2024mechanismofanion pages 1-2). These insights can be extrapolated to bacterial SulP homologs for tool compound development to probe function in SRB.
- Pathway modeling in SRB: Comparative genomics outlines the transporter complements (SulP, CysZ; often multiple paralogs) and informs metabolic models of sulfate uptake constraints in SRM, with implications for biogeochemical cycling and bioprocesses (marietou2018sulfatetransportersin pages 1-2, marietou2018sulfatetransportersin pages 3-4, marietou2018sulfatetransportersin pages 2-3).

4) Expert opinions and analysis from authoritative sources
- Transport energetics in SRB: Because dissimilatory sulfate reduction has narrow energetic margins—two ATP are consumed to activate sulfate (APS formation) while three ATP are produced—ABC-type sulfate uptake (ATP-driven SulT) is unlikely in SRB; instead, secondary-active systems (SulP, DASS, CysZ) are favored (marietou2018sulfatetransportersin pages 4-6). This analysis supports assigning DVU_0279 to a secondary-active transporter role rather than ATP-driven import.
- Family-level mechanism: The 2024 SLC26A4 structures provide an authoritative update that SLC26 exchangers utilize multiple anion-binding sites and STAS-domain regulation, a model likely conserved in bacterial SulP transporters (wang2024mechanismofanion pages 1-2).

5) Relevant statistics and data from recent studies
- Transporter family prevalence in SRM genomes: Across 44 SRM genomes surveyed, the average counts were approximately SulP (2), DASS (3), CysP (1), and CysZ (8) per genome, with CysZ present in all genomes examined (marietou2018sulfatetransportersin pages 2-3). SulP absence correlates with high-temperature specialists (marietou2018sulfatetransportersin pages 3-4).
- D. vulgaris Hildenborough SulP set: Three SulP-type transporters are noted (DVU0053, DVU0279, DVU1999). DVU0279 clusters phylogenetically with dicarboxylate transporter DauA, while DVU1999 clusters with bicarbonate transporters; DVU0053 is the best candidate for a sulfate-selective SulP. None of these three are essential for sulfate uptake in physiological studies and/or transposon studies, implying alternative uptake routes (e.g., CysZ) (marietou2018sulfatetransportersin pages 16-17).

Functional annotation for DVU_0279 (Q72FD5)
- Likely molecular function: Secondary-active anion transporter of the SulP/SLC26 family with a cytosolic STAS regulatory domain. Given its phylogenetic clustering with the dicarboxylate transporter DauA, DVU_0279 may prefer dicarboxylates and/or related anions, rather than being a high-affinity sulfate importer per se (marietou2018sulfatetransportersin pages 16-17). Family-level behavior supports capabilities for anion exchange or symport (e.g., Cl−/HCO3−, SO4^2−/H+), but precise substrate specificity for DVU_0279 remains to be experimentally resolved (wang2024mechanismofanion pages 1-2, marietou2018sulfatetransportersin pages 20-20).
- Substrate specificity (inference strength): Moderate, based on phylogenetic placement and family properties. DVU_0279’s DauA-like clustering suggests potential for C4-dicarboxylates (e.g., succinate/fumarate) or other di-anions; within the SulP family, other members transport sulfate, bicarbonate, oxalate, and halides (marietou2018sulfatetransportersin pages 16-17, wang2024mechanismofanion pages 1-2, marietou2018sulfatetransportersin pages 20-20).
- Cellular localization: Inner (cytoplasmic) membrane integral transporter with cytosolic STAS tail, by homology to SulP/SLC26 architecture (marietou2018sulfatetransportersin pages 20-20, wang2024mechanismofanion pages 1-2).
- Pathway role in D. vulgaris Hildenborough: Not strictly essential for sulfate uptake; DvH encodes multiple uptake systems, notably numerous CysZ transporters, which are ubiquitous across SRM and likely contribute significantly to sulfate import. DVU0053 is the better SulP candidate for sulfate uptake, while DVU0279 may fulfill a broader anion/dicarboxylate transport role that supports central metabolism under specific conditions (marietou2018sulfatetransportersin pages 16-17, marietou2018sulfatetransportersin pages 1-2, marietou2018sulfatetransportersin pages 2-3).
- Regulation: The STAS domain in SLC26/SulP transporters influences anion exchange through interactions with the transmembrane domain; this likely applies to DVU_0279, affecting gating/affinity and potentially partner interactions (wang2024mechanismofanion pages 1-2, marietou2018sulfatetransportersin pages 20-20).

Sulfate uptake systems in SRB and D. vulgaris
- Families implicated: SulP and CysZ families are most consistently implicated in SRM sulfate uptake; ABC-type SulT is typically not used by SRM. Both Na+- and H+-coupled symporters exist in SRM, indicating flexibility in coupling ions (marietou2018sulfatetransportersin pages 1-2, marietou2018sulfatetransportersin pages 3-4, marietou2018sulfatetransportersin pages 2-3).
- Energetic constraints: Because SRB conserve little net ATP per sulfate reduced, ATP-driven sulfate import is disfavored; this underpins reliance on secondary-active uptake (marietou2018sulfatetransportersin pages 4-6).

Evidence caveats and recommendations
- Ambiguity and limits: Direct experimental characterization of DVU_0279 substrate specificity in DvH was not located in recent literature. The best organism-specific evidence is comparative genomics that places DVU_0279 with DauA-like transporters and indicates it is not essential for sulfate uptake. Therefore, functional annotation should be reported as “putative SulP/SLC26 anion transporter, possibly dicarboxylate-inclined” and not as a confirmed sulfate transporter (marietou2018sulfatetransportersin pages 16-17).
- Next steps: Combine targeted genetics (clean deletion or CRISPRi of DVU_0279 with growth on specific anions), radiolabeled or electrophysiological uptake assays, and heterologous expression reconstitution. Use recent SLC26 mechanistic insights (dual anion-binding sites, STAS–TMD interactions) to design mutagenesis of predicted binding/stabilizing residues (wang2024mechanismofanion pages 1-2).

References (with URLs and dates)
- Wang L. et al. Mechanism of anion exchange and small-molecule inhibition of pendrin (SLC26A4). Nature Communications. 2024-01-09. https://doi.org/10.1038/s41467-023-44612-1 (wang2024mechanismofanion pages 1-2).
- Marietou A. et al. Sulfate Transporters in Dissimilatory Sulfate Reducing Microorganisms: A Comparative Genomics Analysis. Frontiers in Microbiology. 2018-03-02. https://doi.org/10.3389/fmicb.2018.00309 (marietou2018sulfatetransportersin pages 16-17, marietou2018sulfatetransportersin pages 1-2, marietou2018sulfatetransportersin pages 4-6, marietou2018sulfatetransportersin pages 20-20, marietou2018sulfatetransportersin pages 3-4, marietou2018sulfatetransportersin pages 2-3).
- Kuhn B.T. et al. SLC26A11 is an atypical solute carrier with dual transport-channel function mediating lysosomal sulfate transport. bioRxiv. 2025-08-17. https://doi.org/10.1101/2025.08.17.670773 (contextual mechanism; outside 2023–2024 priority) (kuhn2025slc26a11isan pages 1-4).

Conclusion
Q72FD5 (DVU_0279) in Desulfovibrio vulgaris Hildenborough is a SulP/SLC26-family inner-membrane anion transporter with a regulatory STAS domain. Organism-specific comparative genomics places it with DauA-like dicarboxylate transporters, and it is not essential for sulfate uptake in DvH, which likely relies heavily on CysZ and possibly other SulP paralogs (DVU0053) for sulfate import. Recent 2024 structures of an SLC26 member (pendrin) clarify conserved SLC26 mechanisms that likely extend to DVU_0279, including multi-site anion coordination and STAS–TMD regulatory coupling. Experimental determination of DVU_0279’s substrate profile in DvH remains a key gap and should be addressed with targeted functional assays (marietou2018sulfatetransportersin pages 16-17, marietou2018sulfatetransportersin pages 1-2, wang2024mechanismofanion pages 1-2, marietou2018sulfatetransportersin pages 4-6, marietou2018sulfatetransportersin pages 20-20, marietou2018sulfatetransportersin pages 3-4, marietou2018sulfatetransportersin pages 2-3).

References

1. (marietou2018sulfatetransportersin pages 1-2): Angeliki Marietou, Hans Røy, Bo B. Jørgensen, and Kasper U. Kjeldsen. Sulfate transporters in dissimilatory sulfate reducing microorganisms: a comparative genomics analysis. Frontiers in Microbiology, Mar 2018. URL: https://doi.org/10.3389/fmicb.2018.00309, doi:10.3389/fmicb.2018.00309. This article has 83 citations and is from a poor quality or predatory journal.

2. (marietou2018sulfatetransportersin pages 20-20): Angeliki Marietou, Hans Røy, Bo B. Jørgensen, and Kasper U. Kjeldsen. Sulfate transporters in dissimilatory sulfate reducing microorganisms: a comparative genomics analysis. Frontiers in Microbiology, Mar 2018. URL: https://doi.org/10.3389/fmicb.2018.00309, doi:10.3389/fmicb.2018.00309. This article has 83 citations and is from a poor quality or predatory journal.

3. (marietou2018sulfatetransportersin pages 16-17): Angeliki Marietou, Hans Røy, Bo B. Jørgensen, and Kasper U. Kjeldsen. Sulfate transporters in dissimilatory sulfate reducing microorganisms: a comparative genomics analysis. Frontiers in Microbiology, Mar 2018. URL: https://doi.org/10.3389/fmicb.2018.00309, doi:10.3389/fmicb.2018.00309. This article has 83 citations and is from a poor quality or predatory journal.

4. (wang2024mechanismofanion pages 1-2): Lie Wang, Anthony Hoang, Eva Gil-Iturbe, Arthur Laganowsky, Matthias Quick, and Ming Zhou. Mechanism of anion exchange and small-molecule inhibition of pendrin. Nature Communications, Jan 2024. URL: https://doi.org/10.1038/s41467-023-44612-1, doi:10.1038/s41467-023-44612-1. This article has 19 citations and is from a highest quality peer-reviewed journal.

5. (marietou2018sulfatetransportersin pages 3-4): Angeliki Marietou, Hans Røy, Bo B. Jørgensen, and Kasper U. Kjeldsen. Sulfate transporters in dissimilatory sulfate reducing microorganisms: a comparative genomics analysis. Frontiers in Microbiology, Mar 2018. URL: https://doi.org/10.3389/fmicb.2018.00309, doi:10.3389/fmicb.2018.00309. This article has 83 citations and is from a poor quality or predatory journal.

6. (marietou2018sulfatetransportersin pages 2-3): Angeliki Marietou, Hans Røy, Bo B. Jørgensen, and Kasper U. Kjeldsen. Sulfate transporters in dissimilatory sulfate reducing microorganisms: a comparative genomics analysis. Frontiers in Microbiology, Mar 2018. URL: https://doi.org/10.3389/fmicb.2018.00309, doi:10.3389/fmicb.2018.00309. This article has 83 citations and is from a poor quality or predatory journal.

7. (kuhn2025slc26a11isan pages 1-4): Benedikt T Kuhn, Peter Kovermann, Bassam G Haddad, Tim Rasmussen, Tamsanga Hove, Stefanie Bungert-Pluemke, Bettina Boettcher, Jan-Philipp Machtens, Christoph Fahlke, and Eric R. Geertsma. Slc26a11 is an atypical solute carrier with dual transport-channel function mediating lysosomal sulfate transport. BioRxiv, Aug 2025. URL: https://doi.org/10.1101/2025.08.17.670773, doi:10.1101/2025.08.17.670773. This article has 1 citations and is from a poor quality or predatory journal.

8. (marietou2018sulfatetransportersin pages 4-6): Angeliki Marietou, Hans Røy, Bo B. Jørgensen, and Kasper U. Kjeldsen. Sulfate transporters in dissimilatory sulfate reducing microorganisms: a comparative genomics analysis. Frontiers in Microbiology, Mar 2018. URL: https://doi.org/10.3389/fmicb.2018.00309, doi:10.3389/fmicb.2018.00309. This article has 83 citations and is from a poor quality or predatory journal.

Citations

1. marietou2018sulfatetransportersin pages 16-17
2. wang2024mechanismofanion pages 1-2
3. marietou2018sulfatetransportersin pages 20-20
4. marietou2018sulfatetransportersin pages 4-6
5. marietou2018sulfatetransportersin pages 2-3
6. marietou2018sulfatetransportersin pages 3-4
7. marietou2018sulfatetransportersin pages 1-2
8. https://doi.org/10.1038/s41467-023-44612-1
9. https://doi.org/10.3389/fmicb.2018.00309
10. https://doi.org/10.1101/2025.08.17.670773
11. https://doi.org/10.3389/fmicb.2018.00309,
12. https://doi.org/10.1038/s41467-023-44612-1,
13. https://doi.org/10.1101/2025.08.17.670773,