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{
"metadata": {
"accession": "IPR011495",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF07568": "Histidine kinase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR011495",
"name": "Signal transduction histidine kinase, subgroup 2, dimerisation and phosphoacceptor domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Signal transduction histidine kinase, subgroup 2, dimerisation and phosphoacceptor domain",
"short": "Sig_transdc_His_kin_sub2_dim/P"
},
"description": [
{
"text": "<p>This is the dimerisation and phosphoacceptor domain of a subfamily of histidine kinases. It shares sequence similarity with [interpro:IPR003661] and [interpro:IPR011102]. It is usually found adjacent to a C-terminal ATPase domain ([interpro:IPR003594]). This domain is found in a wide range of bacteria and also several archaea.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [[cite:PUB00042804]]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [[cite:PUB00042805]]. These pathways have been adapted to response to a wide variety of stimuli, including nutrients, cellular redox state, changes in osmolarity, quorum signals, antibiotics, and more [[cite:PUB00010651]]. Two-component systems are comprised of a sensor histidine kinase (HK) and its cognate response regulator (RR) [[cite:PUB00011096]]. The HK catalyses its own auto-phosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, which can then effect changes in cellular physiology, often by regulating gene expression. Some HK are bifunctional, catalysing both the phosphorylation and dephosphorylation of their cognate RR. The input stimuli can regulate either the kinase or phosphatase activity of the bifunctional HK.</p>\r\n<p>A variant of the two-component system is the phospho-relay system. Here a hybrid HK auto-phosphorylates and then transfers the phosphoryl group to an internal receiver domain, rather than to a separate RR protein. The phosphoryl group is then shuttled to histidine phosphotransferase (HPT) and subsequently to a terminal RR, which can evoke the desired response [[cite:PUB00042806], [cite:PUB00042807]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Signal transducing histidine kinases are the key elements in two-component signal transduction systems, which control complex processes such as the initiation of development in microorganisms [[cite:PUB00013246], [cite:PUB00007866]]. Examples of histidine kinases are EnvZ, which plays a central role in osmoregulation [[cite:PUB00013247]], and CheA, which plays a central role in the chemotaxis system [[cite:PUB00000966]]. Histidine kinases usually have an N-terminal ligand-binding domain and a C-terminal kinase domain, but other domains may also be present. The kinase domain is responsible for the autophosphorylation of the histidine with ATP, the phosphotransfer from the kinase to an aspartate of the response regulator, and (with bifunctional enzymes) the phosphotransfer from aspartyl phosphate back to ADP or to water [[cite:PUB00020801]]. The kinase core has a unique fold, distinct from that of the Ser/Thr/Tyr kinase superfamily.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00042804": {
"PMID": 16176121,
"ISBN": null,
"volume": "3",
"issue": "10",
"year": 2005,
"title": "Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis.",
"URL": null,
"raw_pages": "e334",
"medline_journal": "PLoS Biol",
"ISO_journal": "PLoS Biol.",
"authors": [
"Skerker JM",
"Prasol MS",
"Perchuk BS",
"Biondi EG",
"Laub MT."
],
"DOI_URL": "http://dx.doi.org/10.1371/journal.pbio.0030334"
},
"PUB00042805": {
"PMID": 18076326,
"ISBN": null,
"volume": "41",
"issue": null,
"year": 2007,
"title": "Specificity in two-component signal transduction pathways.",
"URL": null,
"raw_pages": "121-45",
"medline_journal": "Annu Rev Genet",
"ISO_journal": "Annu. Rev. Genet.",
"authors": [
"Laub MT",
"Goulian M."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.genet.41.042007.170548"
},
"PUB00010651": {
"PMID": 12372152,
"ISBN": null,
"volume": "3",
"issue": "10",
"year": 2002,
"title": "Histidine protein kinases: key signal transducers outside the animal kingdom.",
"URL": null,
"raw_pages": "REVIEWS3013",
"medline_journal": "Genome Biol",
"ISO_journal": "Genome Biol.",
"authors": [
"Wolanin PM",
"Thomason PA",
"Stock JB."
],
"DOI_URL": "http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=12372152"
},
"PUB00011096": {
"PMID": 10966457,
"ISBN": null,
"volume": "69",
"issue": null,
"year": 2000,
"title": "Two-component signal transduction.",
"URL": null,
"raw_pages": "183-215",
"medline_journal": "Annu Rev Biochem",
"ISO_journal": "Annu. Rev. Biochem.",
"authors": [
"Stock AM",
"Robinson VL",
"Goudreau PN."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.biochem.69.1.183"
},
"PUB00042806": {
"PMID": 11934609,
"ISBN": null,
"volume": "5",
"issue": "2",
"year": 2002,
"title": "Molecular recognition of bacterial phosphorelay proteins.",
"URL": null,
"raw_pages": "142-8",
"medline_journal": "Curr Opin Microbiol",
"ISO_journal": "Curr. Opin. Microbiol.",
"authors": [
"Varughese KI."
],
"DOI_URL": "http://dx.doi.org/10.1016/S1369-5274(02)00305-3"
},
"PUB00042807": {
"PMID": 11489844,
"ISBN": null,
"volume": "183",
"issue": "17",
"year": 2001,
"title": "Keeping signals straight in phosphorelay signal transduction.",
"URL": null,
"raw_pages": "4941-9",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Hoch JA",
"Varughese KI."
],
"DOI_URL": "http://dx.doi.org/10.1128/JB.183.17.4941-4949.2001"
},
"PUB00013246": {
"PMID": 8868347,
"ISBN": null,
"volume": "12",
"issue": "3",
"year": 1996,
"title": "Protein aspartate phosphatases control the output of two-component signal transduction systems.",
"URL": null,
"raw_pages": "97-101",
"medline_journal": "Trends Genet",
"ISO_journal": "Trends Genet.",
"authors": [
"Perego M",
"Hoch JA."
],
"DOI_URL": "http://dx.doi.org/10.1016/0168-9525(96)81420-X"
},
"PUB00007866": {
"PMID": 11406410,
"ISBN": null,
"volume": "26",
"issue": "6",
"year": 2001,
"title": "Histidine kinases and response regulator proteins in two-component signaling systems.",
"URL": null,
"raw_pages": "369-76",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"West AH",
"Stock AM."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0968-0004(01)01852-7"
},
"PUB00013247": {
"PMID": 10426948,
"ISBN": null,
"volume": "6",
"issue": "8",
"year": 1999,
"title": "Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ.",
"URL": null,
"raw_pages": "729-34",
"medline_journal": "Nat Struct Biol",
"ISO_journal": "Nat. Struct. Biol.",
"authors": [
"Tomomori C",
"Tanaka T",
"Dutta R",
"Park H",
"Saha SK",
"Zhu Y",
"Ishima R",
"Liu D",
"Tong KI",
"Kurokawa H",
"Qian H",
"Inouye M",
"Ikura M."
],
"DOI_URL": "http://dx.doi.org/10.1038/11495"
},
"PUB00000966": {
"PMID": 9989504,
"ISBN": null,
"volume": "96",
"issue": "1",
"year": 1999,
"title": "Structure of CheA, a signal-transducing histidine kinase.",
"URL": null,
"raw_pages": "131-41",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Bilwes AM",
"Alex LA",
"Crane BR",
"Simon MI."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0092-8674(00)80966-6"
},
"PUB00020801": {
"PMID": 11145881,
"ISBN": null,
"volume": "11",
"issue": "6",
"year": 2000,
"title": "Bacteriophytochromes: new tools for understanding phytochrome signal transduction.",
"URL": null,
"raw_pages": "511-21",
"medline_journal": "Semin Cell Dev Biol",
"ISO_journal": "Semin. Cell Dev. Biol.",
"authors": [
"Vierstra RD",
"Davis SJ."
],
"DOI_URL": "http://dx.doi.org/10.1006/scdb.2000.0206"
},
"PUB00013562": {
"PMID": 8029829,
"ISBN": null,
"volume": "10",
"issue": "4",
"year": 1994,
"title": "Protein histidine kinases and signal transduction in prokaryotes and eukaryotes.",
"URL": null,
"raw_pages": "133-8",
"medline_journal": "Trends Genet",
"ISO_journal": "Trends Genet.",
"authors": [
"Alex LA",
"Simon MI."
],
"DOI_URL": "http://dx.doi.org/10.1016/0168-9525(94)90215-1"
},
"PUB00013563": {
"PMID": 1482126,
"ISBN": null,
"volume": "26",
"issue": null,
"year": 1992,
"title": "Communication modules in bacterial signaling proteins.",
"URL": null,
"raw_pages": "71-112",
"medline_journal": "Annu Rev Genet",
"ISO_journal": "Annu. Rev. Genet.",
"authors": [
"Parkinson JS",
"Kofoid EC."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.ge.26.120192.000443"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 1351,
"interactions": 0,
"matches": 19021,
"pathways": 0,
"proteins": 19021,
"proteomes": 7831,
"sets": 0,
"structural_models": {
"alphafold": 13918,
"bfvd": 0
},
"structures": 2,
"taxa": 12075
},
"entry_annotations": {
"alignment:seed": 64,
"alignment:full": 7696
},
"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": "GenProp0292",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0292"
}
]
},
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "2.7.13.3",
"url": "https://enzyme.expasy.org/EC/2.7.13.3"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
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"representative_structure": null
}
}
