Summary: Bacterial transcriptional regulator
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Bacterial transcriptional regulator Provide feedback
This family of bacterial transcriptional regulators includes the glycerol operon regulatory protein and acetate operon repressor both of which are members of the iclR family. These proteins have a Helix-Turn-Helix motif at the N-terminus. However this family covers the C-terminal region that may bind to the regulatory substrate (unpublished observation, Bateman A.).
Galinier A, Bleicher F, Negre D, Perriere G, Duclos B, Cozzone AJ, Cortay JC; , Gene 1991;97:149-150.: Primary structure of the intergenic region between aceK and iclR in the Escherichia coli chromosome. PUBMED:1995429 EPMC:1995429
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR014757
The many bacterial transcription regulation proteins which bind DNA through a 'helix-turn-helix' motif can be classified into subfamilies on the basis of sequence similarities. One of these subfamilies, called 'iclR', groups several proteins including:
- gylR, a possible activator protein for the gylABX glycerol operon in Streptomyces.
- iclR, the repressor of the acetate operon (also known as glyoxylate bypass operon) in Escherichia coli and Salmonella typhimurium.
These proteins have a Helix-Turn-Helix motif at the N terminus that is similar to that of other DNA-binding proteins [PUBMED:1840643].
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Curation and family details
|Seed source:||Pfam-B_755 (release 4.1)|
|Author:||Bashton M, Bateman A|
|Number in seed:||23|
|Number in full:||10733|
|Average length of the domain:||124.00 aa|
|Average identity of full alignment:||23 %|
|Average coverage of the sequence by the domain:||46.91 %|
|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:||13|
|Download:||download the raw HMM for this family|
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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 IclR domain has been found. There are 47 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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