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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR010242",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0003690",
"name": "double-stranded DNA binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0003700",
"name": "DNA-binding transcription factor activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006355",
"name": "regulation of DNA-templated transcription",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"hamap": {
"MF_01176": "HTH-type transcriptional regulator IscR [iscR]"
},
"ncbifam": {
"TIGR02010": "Fe-S cluster assembly transcriptional regulator IscR"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR000944",
"name": "Transcription regulator Rrf2",
"type": "Family",
"children": [
{
"accession": "IPR010242",
"name": "Transcription factor HTH, IscR",
"type": "Family",
"children": []
},
{
"accession": "IPR014290",
"name": "SUF system FeS cluster assembly regulator",
"type": "Family",
"children": []
},
{
"accession": "IPR023761",
"name": "Transcriptional repressor HTH, NsrR",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Transcription factor HTH, IscR",
"short": "TF_HTH_IscR"
},
"description": [
{
"text": "<p>This entry describes IscR, an iron-sulphur binding transcription factor of the ISC iron-sulphur cluster assembly system [[cite:PUB00033785]]. The HTH-type transcriptional regulator IscR (iron-sulphur cluster regulator) regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. It is a transcriptional repressor of the iscRSUA operon, which is involved in the assembly of Fe-S clusters into Fe-S proteins. In its apoform, under conditions of oxidative stress or iron deprivation, it activates the suf operon, which is a second operon involved in the assembly of Fe-S clusters. It represses its own transcription [[cite:PUB00033785], [cite:PUB00054980]]. It is induced by oxidative stress conditions and iron starvation [[cite:PUB00043090]].</p>",
"llm": false,
"checked": false,
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},
{
"text": "<p>Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S] and [4Fe-4S] [[cite:PUB00035635]]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S] form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far in bacteria, three FeS assembly machineries have been identified that are capable of synthesising all types of [Fe-S] clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.</p>\n\n<p>The ISC system is conserved in eubacteria and eukaryotes (mitochondria) and has broad specificity, targeting general FeS proteins [[cite:PUB00035636], [cite:PUB00035637]]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transferring them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [[cite:PUB00035638]].</p>\n\n<p>The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA [[cite:PUB00035639]]. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [[cite:PUB00035640]], acting as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoprotein targets.</p>\n\n<p>In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins [[cite:PUB00028014]]. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [[cite:PUB00003442]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00043090": {
"PMID": 16677314,
"ISBN": null,
"volume": "60",
"issue": "4",
"year": 2006,
"title": "IscR-dependent gene expression links iron-sulphur cluster assembly to the control of O2-regulated genes in Escherichia coli.",
"URL": null,
"raw_pages": "1058-75",
"medline_journal": "Mol Microbiol",
"ISO_journal": "Mol. Microbiol.",
"authors": [
"Giel JL",
"Rodionov D",
"Liu M",
"Blattner FR",
"Kiley PJ."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1365-2958.2006.05160.x"
},
"PUB00028014": {
"PMID": 11498000,
"ISBN": null,
"volume": "29",
"issue": "Pt 4",
"year": 2001,
"title": "Incorporation of iron-sulphur clusters in membrane-bound proteins.",
"URL": null,
"raw_pages": "418-21",
"medline_journal": "Biochem Soc Trans",
"ISO_journal": "Biochem. Soc. Trans.",
"authors": [
"Seidler A",
"Jaschkowitz K",
"Wollenberg M."
],
"DOI_URL": "http://www.biochemsoctrans.org/bst/029/0418/0290418.pdf"
},
"PUB00054980": {
"PMID": 16824106,
"ISBN": null,
"volume": "61",
"issue": "1",
"year": 2006,
"title": "IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins.",
"URL": null,
"raw_pages": "206-18",
"medline_journal": "Mol Microbiol",
"ISO_journal": "Mol. Microbiol.",
"authors": [
"Yeo WS",
"Lee JH",
"Lee KC",
"Roe JH."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1365-2958.2006.05220.x"
},
"PUB00035638": {
"PMID": 15937904,
"ISBN": null,
"volume": "60",
"issue": "3",
"year": 2005,
"title": "Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters.",
"URL": null,
"raw_pages": "566-9",
"medline_journal": "Proteins",
"ISO_journal": "Proteins",
"authors": [
"Shimomura Y",
"Takahashi Y",
"Kakuta Y",
"Fukuyama K."
],
"DOI_URL": "http://dx.doi.org/10.1002/prot.20481"
},
"PUB00035639": {
"PMID": 17350000,
"ISBN": null,
"volume": "581",
"issue": "7",
"year": 2007,
"title": "The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA.",
"URL": null,
"raw_pages": "1362-8",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Sendra M",
"Ollagnier de Choudens S",
"Lascoux D",
"Sanakis Y",
"Fontecave M."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.febslet.2007.02.058"
},
"PUB00035636": {
"PMID": 16211402,
"ISBN": null,
"volume": "10",
"issue": "7",
"year": 2005,
"title": "Mechanisms of iron-sulfur cluster assembly: the SUF machinery.",
"URL": null,
"raw_pages": "713-21",
"medline_journal": "J Biol Inorg Chem",
"ISO_journal": "J. Biol. Inorg. Chem.",
"authors": [
"Fontecave M",
"Choudens SO",
"Py B",
"Barras F."
],
"DOI_URL": "http://dx.doi.org/10.1007/s00775-005-0025-1"
},
"PUB00033785": {
"PMID": 11742080,
"ISBN": null,
"volume": "98",
"issue": "26",
"year": 2001,
"title": "IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins.",
"URL": null,
"raw_pages": "14895-900",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Schwartz CJ",
"Giel JL",
"Patschkowski T",
"Luther C",
"Ruzicka FJ",
"Beinert H",
"Kiley PJ."
],
"DOI_URL": "http://dx.doi.org/10.1073/pnas.251550898"
},
"PUB00035637": {
"PMID": 16843540,
"ISBN": null,
"volume": "1763",
"issue": "7",
"year": 2006,
"title": "Mechanisms of iron-sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes.",
"URL": null,
"raw_pages": "652-67",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Lill R",
"Dutkiewicz R",
"Elsasser HP",
"Hausmann A",
"Netz DJ",
"Pierik AJ",
"Stehling O",
"Urzica E",
"Muhlenhoff U."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.bbamcr.2006.05.011"
},
"PUB00035635": {
"PMID": 16221578,
"ISBN": null,
"volume": "50",
"issue": null,
"year": 2005,
"title": "How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins.",
"URL": null,
"raw_pages": "41-101",
"medline_journal": "Adv Microb Physiol",
"ISO_journal": "Adv. Microb. Physiol.",
"authors": [
"Barras F",
"Loiseau L",
"Py B."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0065-2911(05)50002-X"
},
"PUB00035640": {
"PMID": 15278785,
"ISBN": null,
"volume": "9",
"issue": "7",
"year": 2004,
"title": "SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly.",
"URL": null,
"raw_pages": "828-38",
"medline_journal": "J Biol Inorg Chem",
"ISO_journal": "J. Biol. Inorg. Chem.",
"authors": [
"Ollagnier-de-Choudens S",
"Sanakis Y",
"Fontecave M."
],
"DOI_URL": "http://dx.doi.org/10.1007/s00775-004-0581-9"
},
"PUB00003442": {
"PMID": 8875867,
"ISBN": null,
"volume": "43",
"issue": "5",
"year": 1996,
"title": "A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.",
"URL": null,
"raw_pages": "536-40",
"medline_journal": "J Mol Evol",
"ISO_journal": "J. Mol. Evol.",
"authors": [
"Hwang DM",
"Dempsey A",
"Tan KT",
"Liew CC."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036388",
"name": "Winged helix-like DNA-binding domain superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR036390",
"name": "Winged helix DNA-binding domain superfamily",
"type": "homologous_superfamily"
}
],
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"structural_models": {
"alphafold": 3260,
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"taxa": 4716
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"entry_annotations": {},
"cross_references": {
"gp": {
"displayName": "Genome Properties",
"description": "Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.",
"rank": 45,
"accessions": [
{
"accession": "GenProp0138",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0138"
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}
