HMPREF1058_RS08555 is a large membrane-associated regulatory protein containing a helix-turn-helix (HTH) LuxR-type DNA-binding domain. This 798-amino acid protein functions as a transcriptional regulator controlling genes involved in phosphosugar metabolism and growth responses. The protein contains a signal peptide, multiple transmembrane domains, and structural similarities to quinoprotein alcohol dehydrogenase-like proteins, suggesting it may have dual regulatory and enzymatic functions. This protein represents an important regulatory component in Bacteroidetes metabolism, particularly for adapting to different carbon sources in the gut environment.
Definition: The process of controlling the expression of genes involved in the uptake, transport, and catabolism of phosphorylated sugars in bacterial cells
Justification: Specific regulatory process not captured by existing GO terms, important for bacterial adaptation to different carbohydrate sources
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
|
GO:0016020
membrane
|
IEA
UniProt:I9U7L5 |
NEW |
Summary: Correct cellular location - protein contains signal peptide and transmembrane domains
Reason: UniProt annotations show membrane localization supported by signal peptide prediction and transmembrane domain analysis. Not in GOA but present in UniProt DR section.
|
|
GO:0003700
DNA-binding transcription factor activity
|
TAS
UniProt:I9U7L5 |
NEW |
Summary: Core molecular function - HTH LuxR-type domain indicates transcriptional regulatory activity
Reason: The HTH LuxR-type domain is characteristic of DNA-binding transcriptional regulators that control gene expression.
|
|
GO:0006355
regulation of DNA-templated transcription
|
TAS
UniProt:I9U7L5 |
NEW |
Summary: Core biological process - transcriptional regulator controlling phosphosugar metabolism
Reason: As a LuxR-type transcriptional regulator, this protein is involved in controlling transcription of target genes.
|
Q: What specific genes and pathways are regulated by this LuxR-type protein in phosphosugar metabolism?
Suggested experts: Bacterial metabolism researchers, Transcriptional regulation specialists, Systems biology experts
Q: How does this protein integrate environmental signals to control transcriptional responses?
Suggested experts: Signal transduction researchers, Bacterial physiology specialists, Regulatory network analysts
Q: What is the evolutionary relationship between this protein and other LuxR-type regulators in Bacteroidetes?
Suggested experts: Comparative genomics researchers, Bacterial evolution specialists, Phylogenetic analysis experts
Q: Does this protein have enzymatic activity in addition to its regulatory function?
Suggested experts: Enzyme biochemists, Protein function specialists, Structural biologists
Experiment: RNA-seq analysis of wild-type vs knockout strains under different carbon source conditions to identify regulated genes and pathways.
Type: Transcriptional profiling
Experiment: ChIP-seq or EMSA experiments to identify direct DNA-binding targets and consensus recognition sequences for the HTH domain.
Type: DNA-binding specificity analysis
Experiment: Systematic growth analysis on various phosphosugars and carbon sources to determine the regulatory role in metabolism.
Type: Growth phenotype characterization
Experiment: X-ray crystallography or cryo-EM structure of the full-length protein to understand the relationship between regulatory and potential enzymatic domains.
Type: Protein structure determination
id: I9U7L5
gene_symbol: HMPREF1058_RS08555
aliases:
- HMPREF1058_02242
- HTH luxR-type domain-containing protein
taxon:
id: NCBITaxon:997891
label: Phocaeicola vulgatus CL09T03C04
description: HMPREF1058_RS08555 is a large membrane-associated regulatory protein
containing a helix-turn-helix (HTH) LuxR-type DNA-binding domain. This 798-amino
acid protein functions as a transcriptional regulator controlling genes involved
in phosphosugar metabolism and growth responses. The protein contains a signal peptide,
multiple transmembrane domains, and structural similarities to quinoprotein alcohol
dehydrogenase-like proteins, suggesting it may have dual regulatory and enzymatic
functions. This protein represents an important regulatory component in Bacteroidetes
metabolism, particularly for adapting to different carbon sources in the gut environment.
existing_annotations:
- term:
id: GO:0016020
label: membrane
evidence_type: IEA
original_reference_id: UniProt:I9U7L5
review:
summary: Correct cellular location - protein contains signal peptide and transmembrane
domains
action: NEW
reason: UniProt annotations show membrane localization supported by signal peptide
prediction and transmembrane domain analysis. Not in GOA but present in UniProt
DR section.
- term:
id: GO:0003700
label: DNA-binding transcription factor activity
evidence_type: TAS
original_reference_id: UniProt:I9U7L5
review:
summary: Core molecular function - HTH LuxR-type domain indicates transcriptional
regulatory activity
action: NEW
reason: The HTH LuxR-type domain is characteristic of DNA-binding transcriptional
regulators that control gene expression.
- term:
id: GO:0006355
label: regulation of DNA-templated transcription
evidence_type: TAS
original_reference_id: UniProt:I9U7L5
review:
summary: Core biological process - transcriptional regulator controlling phosphosugar
metabolism
action: NEW
reason: As a LuxR-type transcriptional regulator, this protein is involved in
controlling transcription of target genes.
core_functions:
- description: HTH LuxR-type transcriptional regulator controlling phosphosugar metabolism
and growth adaptation in gut bacteria
molecular_function:
id: GO:0003700
label: DNA-binding transcription factor activity
directly_involved_in:
- id: GO:0006355
label: regulation of DNA-templated transcription
supported_by:
- reference_id: UniProt:I9U7L5
supporting_text: HTH luxR-type domain-containing protein
proposed_new_terms:
- proposed_name: phosphosugar metabolism regulation
proposed_definition: The process of controlling the expression of genes involved
in the uptake, transport, and catabolism of phosphorylated sugars in bacterial
cells
justification: Specific regulatory process not captured by existing GO terms, important
for bacterial adaptation to different carbohydrate sources
suggested_experiments:
- experiment_type: Transcriptional profiling
description: RNA-seq analysis of wild-type vs knockout strains under different carbon
source conditions to identify regulated genes and pathways.
- experiment_type: DNA-binding specificity analysis
description: ChIP-seq or EMSA experiments to identify direct DNA-binding targets
and consensus recognition sequences for the HTH domain.
- experiment_type: Growth phenotype characterization
description: Systematic growth analysis on various phosphosugars and carbon sources
to determine the regulatory role in metabolism.
- experiment_type: Protein structure determination
description: X-ray crystallography or cryo-EM structure of the full-length protein
to understand the relationship between regulatory and potential enzymatic domains.
suggested_questions:
- question: What specific genes and pathways are regulated by this LuxR-type protein
in phosphosugar metabolism?
experts:
- Bacterial metabolism researchers
- Transcriptional regulation specialists
- Systems biology experts
- question: How does this protein integrate environmental signals to control transcriptional
responses?
experts:
- Signal transduction researchers
- Bacterial physiology specialists
- Regulatory network analysts
- question: What is the evolutionary relationship between this protein and other LuxR-type
regulators in Bacteroidetes?
experts:
- Comparative genomics researchers
- Bacterial evolution specialists
- Phylogenetic analysis experts
- question: Does this protein have enzymatic activity in addition to its regulatory
function?
experts:
- Enzyme biochemists
- Protein function specialists
- Structural biologists
references:
- id: GO_REF:0000043
title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
findings: []
- id: UniProt:I9U7L5
title: UniProt entry for HTH luxR-type domain-containing protein from Phocaeicola
vulgatus
findings:
- statement: Protein contains HTH LuxR-type DNA-binding domain
supporting_text: HTH luxR-type domain-containing protein
- statement: Protein is membrane-associated with signal peptide
supporting_text: "Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius}"
- statement: Protein shows structural similarity to quinoprotein alcohol dehydrogenase
supporting_text: Quinoprotein alcohol dehydrogenase-like
tags:
- lbnl-favorites
status: COMPLETE