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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR032899",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0032506",
"name": "cytokinetic process",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0030428",
"name": "cell septum",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"source_database": "interpro",
"member_databases": {
"hamap": {
"MF_02021": "Cell division protein DamX [damX]"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR032899",
"name": "Cell division protein DamX",
"type": "Family",
"children": []
},
"name": {
"name": "Cell division protein DamX",
"short": "DamX"
},
"description": [
{
"text": "<p>This entry represents the cell division protein DamX from Enterobacteriaceae. DamX is an inner membrane protein that contributes to the cell constriction process during bacterial cytokinesis. It contains a C-terminal SPOR domain that may act as autonomous septal targeting determinant [[cite:PUB00077003], [cite:PUB00077005]]. DamX localises to the septal ring, but it is non-essential for cell division, and it inhibits cell division when overproduced [[cite:PUB00077032]]. It has been suggested that it may contribute to cell envelope biogenesis or integrity in other ways distinct from its role in cell division [[cite:PUB00065333]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00077003": {
"PMID": 19684127,
"ISBN": null,
"volume": "191",
"issue": "24",
"year": 2009,
"title": "Self-enhanced accumulation of FtsN at Division Sites and Roles for Other Proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction.",
"URL": null,
"raw_pages": "7383-401",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Gerding MA",
"Liu B",
"Bendezu FO",
"Hale CA",
"Bernhardt TG",
"de Boer PA."
],
"DOI_URL": "http://dx.doi.org/10.1128/JB.00811-09"
},
"PUB00065333": {
"PMID": 23290046,
"ISBN": null,
"volume": "52",
"issue": "4",
"year": 2013,
"title": "Nuclear magnetic resonance solution structure of the peptidoglycan-binding SPOR domain from Escherichia coli DamX: insights into septal localization.",
"URL": null,
"raw_pages": "627-39",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Williams KB",
"Yahashiri A",
"Arends SJ",
"Popham DL",
"Fowler CA",
"Weiss DS."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi301609e"
},
"PUB00077032": {
"PMID": 7603433,
"ISBN": null,
"volume": "247",
"issue": "5",
"year": 1995,
"title": "Characterization of three genes in the dam-containing operon of Escherichia coli.",
"URL": null,
"raw_pages": "546-54",
"medline_journal": "Mol Gen Genet",
"ISO_journal": "Mol. Gen. Genet.",
"authors": [
"Lyngstadaas A",
"Lobner-Olesen A",
"Boye E."
],
"DOI_URL": "http://dx.doi.org/10.1007/BF00290345"
},
"PUB00077005": {
"PMID": 19880599,
"ISBN": null,
"volume": "192",
"issue": "1",
"year": 2010,
"title": "Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA.",
"URL": null,
"raw_pages": "242-55",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Arends SJ",
"Williams K",
"Scott RJ",
"Rolong S",
"Popham DL",
"Weiss DS."
],
"DOI_URL": "http://dx.doi.org/10.1128/JB.01244-09"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 1444,
"pathways": 0,
"proteins": 1444,
"proteomes": 416,
"sets": 0,
"structural_models": {
"alphafold": 1253,
"bfvd": 0
},
"structures": 0,
"taxa": 991
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
