HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"metadata": {
"accession": "PS00654",
"entry_id": null,
"type": "conserved_site",
"go_terms": null,
"source_database": "prosite",
"member_databases": null,
"integrated": "IPR001550",
"hierarchy": null,
"name": {
"name": "PRD domain signature",
"short": "PRD_1"
},
"description": [
{
"text": "<p>Transcriptional antiterminators and activators containing phosphoenolpyruvate:\nsugar phosphotransferase system (PTS) regulation domains (PRDs) form a class\nof bacterial regulatory proteins whose activity is modulated by\nphosphorylation. These regulators stimulate the expression of genes and\noperons involved in carbohydrate metabolism. They are characterized by the\npresence of a duplicated regulatory module of ~100 residues that can be\nreversibly phosphorylated on histidyl residues by the PTS. PRDs in\ntranscriptional antiterminators and activators are PTS regulatory targets that\nare (de)phosphorylated in response to the availability of carbon sources\n[[cite:PUB00043695]][[cite:PUB00043696]][[cite:PUB00015024]][[cite:PUB00015026]][[cite:PUB00031497]].\n\nThe PRD domain comprises one and often two highly conserved histidines. It\nforms a compact bundle comprising five helices (alpha1-alpha5). The core of the PRD module consists of two pairs of antiparallel\nhelices making an angle of ~60 degrees. The first pairs contains the\nantiparallel helices alpha1 and alpha4, while the second pair contains alpha2\nand alpha5. The third helix (alpha3) is oriented perpendicularly to alpha5 at\nthe periphery of the bundle. The helices are connected by loops of varying\nlength [[cite:PUB00015024]][[cite:PUB00015026]][[cite:PUB00031497]].\n\nSome proteins known to contain a PRD domain are listed below:\n\n - Escherichia coli bglG, which mediates the positive regulation of the beta-\n glucoside (bgl) operon by functioning as a transcriptional antiterminator.\n - Bacillus subtilis licT, which regulates the expression of operons involved\n in beta-glucoside metabolism.\n - Bacillus subtilis licR, the probable licABCH operon regulator.\n - Bacillus subtilis levR, which regulates the expression of the levanase\n operon (levDEFG and sacC). LevR is composed of two domains: a N-terminal\n section that contains a sigma-54 factor interaction ATP-binding domain and\n a C-terminal bglG-like domain. LevR could be phosphorylated by levD or\n levE.\n - Bacillus subtilis sacT, which regulates the expression of the sucrose\n operon (sacPA). SacT is probably phosphorylated by sacP (EII-scr).\n - Bacillus subtilis sacY, which regulates the expression of the levansucrase\n operon (sacBX). SacY is probably phosphorylated by the sacX protein.\n - Bacillus stearothermophilus mtlR activator.\n - Erwinia chrysanthemi arbG [[cite:PUB00002205]], which is involved in the regulation of a\n beta-glucoside operon. ArbG is probably phosphorylated by arbF (EII-bgl).\n - Lactobacillus casei lacT [[cite:PUB00002306]], involved in the regulation of the lac operon.\n\nAs a signature pattern for the PRD domain, we selected a conserved region that\nincludes a conserved histidine that could be the site of phosphorylation. We\nhave also developed a profile, which covers the entire PRD domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00031497": {
"PMID": 15699035,
"ISBN": null,
"volume": "280",
"issue": "15",
"year": 2005,
"title": "Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.",
"URL": null,
"raw_pages": "14780-9",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Graille M",
"Zhou CZ",
"Receveur-Brechot V",
"Collinet B",
"Declerck N",
"van Tilbeurgh H."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M414642200"
},
"PUB00002205": {
"PMID": 1732212,
"ISBN": null,
"volume": "174",
"issue": "3",
"year": 1992,
"title": "Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans.",
"URL": null,
"raw_pages": "765-77",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"el Hassouni M",
"Henrissat B",
"Chippaux M",
"Barras F."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1732212&action=stream&blobtype=pdf"
},
"PUB00043696": {
"PMID": 9663674,
"ISBN": null,
"volume": "28",
"issue": "5",
"year": 1998,
"title": "PRD--a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria.",
"URL": null,
"raw_pages": "865-74",
"medline_journal": "Mol Microbiol",
"ISO_journal": "Mol. Microbiol.",
"authors": [
"Stulke J",
"Arnaud M",
"Rapoport G",
"Martin-Verstraete I."
],
"DOI_URL": "http://dx.doi.org/10.1046/j.1365-2958.1998.00839.x"
},
"PUB00043695": {
"PMID": 9202047,
"ISBN": null,
"volume": "272",
"issue": "27",
"year": 1997,
"title": "Multiple phosphorylation of SacY, a Bacillus subtilis transcriptional antiterminator negatively controlled by the phosphotransferase system.",
"URL": null,
"raw_pages": "17230-7",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Tortosa P",
"Aymerich S",
"Lindner C",
"Saier MH Jr",
"Reizer J",
"Le Coq D."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.272.27.17230"
},
"PUB00015024": {
"PMID": 11751049,
"ISBN": null,
"volume": "11",
"issue": "6",
"year": 2001,
"title": "Structural insights into the regulation of bacterial signalling proteins containing PRDs.",
"URL": null,
"raw_pages": "685-93",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"van Tilbeurgh H",
"Declerck N."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0959-440X(01)00267-6"
},
"PUB00015026": {
"PMID": 11447120,
"ISBN": null,
"volume": "20",
"issue": "14",
"year": 2001,
"title": "Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator.",
"URL": null,
"raw_pages": "3789-99",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"van Tilbeurgh H",
"Le Coq D",
"Declerck N."
],
"DOI_URL": "http://dx.doi.org/10.1093/emboj/20.14.3789"
},
"PUB00002306": {
"PMID": 9045813,
"ISBN": null,
"volume": "179",
"issue": "5",
"year": 1997,
"title": "The lac operon of Lactobacillus casei contains lacT, a gene coding for a protein of the Bg1G family of transcriptional antiterminators.",
"URL": null,
"raw_pages": "1555-62",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Alpert CA",
"Siebers U."
],
"DOI_URL": "http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=9045813"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 1800,
"pathways": 0,
"proteins": 1800,
"proteomes": 791,
"sets": 0,
"structural_models": {
"alphafold": 1424,
"bfvd": 0
},
"structures": 3,
"taxa": 1505
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
