Q833J1 · TCPF_ENTFA
- ProteinNAD(+) hydrolase TcpF
- GenetcpF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids274 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Virulence factor that suppresses host Toll-like receptor (TLR)-mediated cytokine production upon infection (PubMed:25147569, PubMed:25369374).
Acts as a NAD+ hydrolase (NADase) by catalyzing cleavage of NAD+ into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922).
Interacts with various phosphatidylinositol phosphates, such as phosphatidylinositol 3-phosphate (PtdIns3P), phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P), phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P), phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P) (PubMed:25147569).
Acts as a NAD+ hydrolase (NADase) by catalyzing cleavage of NAD+ into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922).
Interacts with various phosphatidylinositol phosphates, such as phosphatidylinositol 3-phosphate (PtdIns3P), phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P), phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P), phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P) (PubMed:25147569).
Catalytic activity
- H2O + NAD+ = ADP-D-ribose + H+ + nicotinamideThis reaction proceeds in the forward direction.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | NAD+ nucleosidase activity | |
Molecular Function | NAD+ nucleotidase, cyclic ADP-ribose generating | |
Molecular Function | phosphatidylinositol-3,4,5-trisphosphate binding | |
Molecular Function | phosphatidylinositol-3,4-bisphosphate binding | |
Molecular Function | phosphatidylinositol-3,5-bisphosphate binding | |
Molecular Function | phosphatidylinositol-3-phosphate binding | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Molecular Function | phosphatidylinositol-4-phosphate binding | |
Biological Process | NAD catabolic process | |
Biological Process | negative regulation of MyD88-dependent toll-like receptor signaling pathway | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD(+) hydrolase TcpF
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Enterococcaceae > Enterococcus
Accessions
- Primary accessionQ833J1
Proteomes
Phenotypes & Variants
Miscellaneous
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000449144 | 1-274 | NAD+ hydrolase TcpF | |||
Sequence: MSNGKKIFISHSSKDQEYVDAFIQLLKKFGFRTQDIFYSSTIETGVQPGELIFDTIKRELTNQPVMLYFLSDHYYQSIPCLNEMGASWMLSDKHYPIALNNFSMKDMKGVISSERLAIAFNDKTSTNEINCLLKKLSHDTDVQAEPDFELNVEKNIQPFQNKLTQLIRQASYLKPDEKGYFETILSTHRPVYGTAKGVYDCFKLPSLIEPKSLGLDTLSEDESHWLFFFLTWGTFQEGEKVRFKLKKDKAYNNREFSDIGKCKNIYVSYLEKVE |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-140 | TIR | ||||
Sequence: NGKKIFISHSSKDQEYVDAFIQLLKKFGFRTQDIFYSSTIETGVQPGELIFDTIKRELTNQPVMLYFLSDHYYQSIPCLNEMGASWMLSDKHYPIALNNFSMKDMKGVISSERLAIAFNDKTSTNEINCLLKKLSHDT |
Domain
The TIR domain mediates NAD+ hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length274
- Mass (Da)31,799
- Last updated2003-06-01 v1
- ChecksumD10115B1C15B1A7B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE016830 EMBL· GenBank· DDBJ | AAO81706.1 EMBL· GenBank· DDBJ | Genomic DNA |