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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR008640",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0019867",
"name": "outer membrane",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF05658": "YadA head domain repeat (2 copies)"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR008640",
"name": "Trimeric autotransporter adhesin YadA-like, head domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Trimeric autotransporter adhesin YadA-like, head domain",
"short": "Adhesin_Head_dom"
},
"description": [
{
"text": "<p>This entry represents the head domain of YadA. This domain is composed almost solely of β-sheets making a novel nine coiled left-handed parallel β-roll (LPBR), surrounded by a partly disordered (N)-terminal random coil and a C-terminal neck region, which consists of a random coil and a short helix at the start of the stalk domain [[cite:PUB00029784]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>The Yersinia adhesin A (YadA) is a trimeric autotransporter adhesin of enteric yersiniae. It consists of three major domains: a head mediating adherence to host cells, a stalk involved in serum resistance, and an anchor that forms a membrane pore and is responsible for the autotransport function [[cite:PUB00095166]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00029784": {
"PMID": 14765110,
"ISBN": null,
"volume": "23",
"issue": "4",
"year": 2004,
"title": "The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll.",
"URL": null,
"raw_pages": "701-11",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Nummelin H",
"Merckel MC",
"Leo JC",
"Lankinen H",
"Skurnik M",
"Goldman A."
],
"DOI_URL": "http://dx.doi.org/10.1038/sj.emboj.7600100"
},
"PUB00095166": {
"PMID": 17921300,
"ISBN": null,
"volume": "189",
"issue": "24",
"year": 2007,
"title": "A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport.",
"URL": null,
"raw_pages": "9011-9",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Grosskinsky U",
"Schutz M",
"Fritz M",
"Schmid Y",
"Lamparter MC",
"Szczesny P",
"Lupas AN",
"Autenrieth IB",
"Linke D."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR011049",
"name": "Serralysin-like metalloprotease, C-terminal",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 3394,
"interactions": 0,
"matches": 75885,
"pathways": 0,
"proteins": 9694,
"proteomes": 1873,
"sets": 0,
"structural_models": {
"alphafold": 5110,
"bfvd": 16
},
"structures": 17,
"taxa": 4104
},
"entry_annotations": {
"alignment:seed": 248,
"alignment:full": 19823
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "7o23",
"name": "C-terminal head domain of the trimeric autotransporter adhesin BpaC from Burkholderia pseudomallei fused to a GCN4 anchor"
}
}
}