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{
"metadata": {
"accession": "cd14738",
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"source_database": "cdd",
"member_databases": null,
"integrated": null,
"hierarchy": null,
"name": {
"name": "proline-alanine-alanine-arginine (PAAR) domain",
"short": "PAAR_2"
},
"description": [
{
"text": "<p>This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli. [[cite:PUB00105087], [cite:PUB00133795], [cite:PUB00133796], [cite:PUB00133797], [cite:PUB00075433], [cite:PUB00133798], [cite:PUB00133799]]</p>",
"llm": false,
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"literature": {
"PUB00133797": {
"PMID": 23429693,
"ISBN": null,
"volume": "62",
"issue": "Pt 5",
"year": 2013,
"title": "Type VI secretion system regulation as a consequence of evolutionary pressure.",
"URL": null,
"raw_pages": "663-676",
"medline_journal": "J Med Microbiol",
"ISO_journal": "J Med Microbiol",
"authors": [
"Miyata ST",
"Bachmann V",
"Pukatzki S."
],
"DOI_URL": null
},
"PUB00133796": {
"PMID": 22746332,
"ISBN": null,
"volume": "66",
"issue": null,
"year": 2012,
"title": "Structure and regulation of the type VI secretion system.",
"URL": null,
"raw_pages": "453-72",
"medline_journal": "Annu Rev Microbiol",
"ISO_journal": "Annu Rev Microbiol",
"authors": [
"Silverman JM",
"Brunet YR",
"Cascales E",
"Mougous JD."
],
"DOI_URL": null
},
"PUB00105087": {
"PMID": 23925114,
"ISBN": null,
"volume": "500",
"issue": "7462",
"year": 2013,
"title": "PAAR-repeat proteins sharpen and diversify the type VI secretion system spike.",
"URL": null,
"raw_pages": "350-353",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Shneider MM",
"Buth SA",
"Ho BT",
"Basler M",
"Mekalanos JJ",
"Leiman PG."
],
"DOI_URL": null
},
"PUB00133795": {
"PMID": 23925115,
"ISBN": null,
"volume": "500",
"issue": "7462",
"year": 2013,
"title": "Microbiology: a weapon for bacterial warfare.",
"URL": null,
"raw_pages": "284-5",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Filloux A."
],
"DOI_URL": null
},
"PUB00133798": {
"PMID": 18524912,
"ISBN": null,
"volume": "154",
"issue": "Pt 6",
"year": 2008,
"title": "The bacterial type VI secretion machine: yet another player for protein transport across membranes.",
"URL": null,
"raw_pages": "1570-1583",
"medline_journal": "Microbiology (Reading)",
"ISO_journal": "Microbiology (Reading)",
"authors": [
"Filloux A",
"Hachani A",
"Bleves S."
],
"DOI_URL": null
},
"PUB00133799": {
"PMID": 19162533,
"ISBN": null,
"volume": "12",
"issue": "1",
"year": 2009,
"title": "The type VI secretion system: translocation of effectors and effector-domains.",
"URL": null,
"raw_pages": "11-7",
"medline_journal": "Curr Opin Microbiol",
"ISO_journal": "Curr Opin Microbiol",
"authors": [
"Pukatzki S",
"McAuley SB",
"Miyata ST."
],
"DOI_URL": null
},
"PUB00075433": {
"PMID": 18289922,
"ISBN": null,
"volume": "11",
"issue": "1",
"year": 2008,
"title": "Type VI secretion: a beginner's guide.",
"URL": null,
"raw_pages": "3-8",
"medline_journal": "Curr Opin Microbiol",
"ISO_journal": "Curr. Opin. Microbiol.",
"authors": [
"Bingle LE",
"Bailey CM",
"Pallen MJ."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.mib.2008.01.006"
}
},
"set_info": {
"accession": "cl21497",
"name": "PAAR_like"
},
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"counters": {
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"domain_architectures": 0,
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"matches": 1927,
"pathways": 0,
"proteins": 1927,
"proteomes": 1289,
"sets": 1,
"structural_models": {
"alphafold": 1365,
"bfvd": 0
},
"structures": 1,
"taxa": 2393
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
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}
}
