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{
"metadata": {
"accession": "IPR002379",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0015078",
"name": "proton transmembrane transporter activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:1902600",
"name": "proton transmembrane transport",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0033177",
"name": "proton-transporting two-sector ATPase complex, proton-transporting domain",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF00137": "ATP synthase subunit C"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR002379",
"name": "V-ATPase proteolipid subunit C-like domain",
"type": "Domain",
"children": []
},
"name": {
"name": "V-ATPase proteolipid subunit C-like domain",
"short": "ATPase_proteolipid_c-like_dom"
},
"description": [
{
"text": "<p>The F-ATPases (or F1F0-ATPases) and V-ATPases (or V1V0-ATPases) are each composed of two linked complexes: the F1 or V1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the F0 or V0 complex that forms the membrane-spanning pore. The F- and V-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis [[cite:PUB00009752], [cite:PUB00020609]].</p>\r\n\r\n<p>In V-ATPases, there are three proteolipid subunits (c, c' and c'') that form part of the proton-conducting pore, each containing a buried glutamic acid residue that is essential for proton transport, and together they form a hexameric ring spanning the membrane [[cite:PUB00020629], [cite:PUB00020631]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.</p>",
"llm": false,
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}
],
"wikipedia": null,
"literature": {
"PUB00068788": {
"PMID": 1385979,
"ISBN": null,
"volume": "1101",
"issue": "2",
"year": 1992,
"title": "F-type or V-type? The chimeric nature of the archaebacterial ATP synthase.",
"URL": null,
"raw_pages": "232-5",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Schafer G",
"Meyering-Vos M."
],
"DOI_URL": null
},
"PUB00068789": {
"PMID": 9741106,
"ISBN": null,
"volume": "21",
"issue": "1",
"year": 1998,
"title": "F-and V-ATPases in the genus Thermus and related species.",
"URL": null,
"raw_pages": "12-22",
"medline_journal": "Syst Appl Microbiol",
"ISO_journal": "Syst. Appl. Microbiol.",
"authors": [
"Radax C",
"Sigurdsson O",
"Hreggvidsson GO",
"Aichinger N",
"Gruber C",
"Kristjansson JK",
"Stan-Lotter H."
],
"DOI_URL": null
},
"PUB00068786": {
"PMID": 20450191,
"ISBN": null,
"volume": "49",
"issue": "23",
"year": 2010,
"title": "Regulation and isoform function of the V-ATPases.",
"URL": null,
"raw_pages": "4715-23",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Toei M",
"Saum R",
"Forgac M."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi100397s"
},
"PUB00068787": {
"PMID": 18937357,
"ISBN": null,
"volume": "30",
"issue": "11-12",
"year": 2008,
"title": "New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0).",
"URL": null,
"raw_pages": "1096-109",
"medline_journal": "Bioessays",
"ISO_journal": "Bioessays",
"authors": [
"Gruber G",
"Marshansky V."
],
"DOI_URL": "http://dx.doi.org/10.1002/bies.20827"
},
"PUB00020629": {
"PMID": 15951435,
"ISBN": null,
"volume": "280",
"issue": "30",
"year": 2005,
"title": "Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain.",
"URL": null,
"raw_pages": "27896-903",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Inoue T",
"Forgac M."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M504890200"
},
"PUB00056210": {
"PMID": 19783985,
"ISBN": null,
"volume": "16",
"issue": "10",
"year": 2009,
"title": "High-resolution structure of the rotor ring of a proton-dependent ATP synthase.",
"URL": null,
"raw_pages": "1068-73",
"medline_journal": "Nat Struct Mol Biol",
"ISO_journal": "Nat. Struct. Mol. Biol.",
"authors": [
"Pogoryelov D",
"Yildiz O",
"Faraldo-Gomez JD",
"Meier T."
],
"DOI_URL": "http://dx.doi.org/10.1038/nsmb.1678"
},
"PUB00009752": {
"PMID": 11309608,
"ISBN": null,
"volume": "410",
"issue": "6831",
"year": 2001,
"title": "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.",
"URL": null,
"raw_pages": "898-904",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Yasuda R",
"Noji H",
"Yoshida M",
"Kinosita K Jr",
"Itoh H."
],
"DOI_URL": "http://dx.doi.org/10.1038/35073513"
},
"PUB00020609": {
"PMID": 15629643,
"ISBN": null,
"volume": "36",
"issue": "2",
"year": 2005,
"title": "A structural model of the vacuolar ATPase from transmission electron microscopy.",
"URL": null,
"raw_pages": "109-26",
"medline_journal": "Micron",
"ISO_journal": "Micron",
"authors": [
"Wilkens S",
"Zhang Z",
"Zheng Y."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.micron.2004.10.002"
},
"PUB00020604": {
"PMID": 15078220,
"ISBN": null,
"volume": "5",
"issue": "2",
"year": 2004,
"title": "Mechanisms of ATPases--a multi-disciplinary approach.",
"URL": null,
"raw_pages": "89-105",
"medline_journal": "Curr Protein Pept Sci",
"ISO_journal": "Curr. Protein Pept. Sci.",
"authors": [
"Rappas M",
"Niwa H",
"Zhang X."
],
"DOI_URL": "http://dx.doi.org/10.2174/1389203043486874"
},
"PUB00020603": {
"PMID": 15473999,
"ISBN": null,
"volume": "576",
"issue": "1-2",
"year": 2004,
"title": "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"URL": null,
"raw_pages": "1-4",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Cross RL",
"Muller V."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.febslet.2004.08.065"
},
"PUB00020631": {
"PMID": 14635779,
"ISBN": null,
"volume": "35",
"issue": "4",
"year": 2003,
"title": "Structure and function of the vacuolar H+-ATPase: moving from low-resolution models to high-resolution structures.",
"URL": null,
"raw_pages": "337-45",
"medline_journal": "J Bioenerg Biomembr",
"ISO_journal": "J. Bioenerg. Biomembr.",
"authors": [
"Harrison M",
"Durose L",
"Song CF",
"Barratt E",
"Trinick J",
"Jones R",
"Findlay JB."
],
"DOI_URL": "http://dx.doi.org/10.1023/A:1025728915565"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR038662",
"name": "F1F0 ATP synthase subunit C superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR035921",
"name": "F/V-ATP synthase subunit C superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
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"taxa": 61948
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},
"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": "GenProp0128",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0128"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "4f4s",
"name": "Structure of the yeast F1Fo ATPase c10 ring with bound oligomycin"
}
}
}
