Summary: QacR-like protein, C-terminal region
QacR-like protein, C-terminal region Provide feedback
This family features the C-terminal region of a number of proteins that bear similarity to the QacR protein (P23217), a transcriptional regulator of the TetR family. QacR is able to bind various environmental agents, which include a number of cationic lipophilic compounds, and thus regulate the transcription of QacA (P23215), a multidrug efflux pump . The C-terminal region contains the multifaceted, expansive drug-binding pocket, which is composed of several separate, but linked, binding sites .
Grkovic S, Brown MH, Roberts NJ, Paulsen IT, Skurray RA; , J Biol Chem 1998;273:18665-18673.: QacR is a repressor protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA. PUBMED:9660841 EPMC:9660841
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013571
This entry represents the C-terminal domain found in the multidrug-binding transcription regulator QacR (SWISSPROT) from Staphylococcus aureus, which is a member of the TetR (tetracycline-resistance) transcriptional regulator family of proteins. QacR is able to bind various environmental agents, which include a number of cationic lipophilic compounds, and thus regulate the transcription of QacA (SWISSPROT), a multidrug efflux pump [PUBMED:9660841]. The C-terminal region of QacR contains a multifaceted, expansive drug-binding pocket, which is composed of several separate, but linked, binding sites [PUBMED:11739955]. The C-terminal domains of QacR and TetR share a multi-helical, interlocking structure.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||sequence-specific DNA binding transcription factor activity (GO:0003700)|
|Biological process||negative regulation of transcription, DNA-dependent (GO:0045892)|
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This clan features families of transcriptional regulators for multidrug efflux pumps, which belong to the TetR superfamily. They are induced by the presence of a variety of factors, such as antibiotics or organic solvents. The C-terminal region featured in these families is thought to contain the inducer-binding site; the divergent sequences in this region allow for the binding of a variety of different inducers [1-4].
The clan contains the following 9 members:DUF1956 TetR_C TetR_C_2 TetR_C_3 TetR_C_4 TetR_C_5 TetR_C_6 TetR_C_7 TetR_C_9
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_96140 (release 17.0)|
|Number in seed:||3|
|Number in full:||259|
|Average length of the domain:||128.70 aa|
|Average identity of full alignment:||32 %|
|Average coverage of the sequence by the domain:||65.29 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the TetR_C_5 domain has been found. There are 104 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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