{"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,"checked":false,"updated":false}],"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":{"subfamilies":0,"domain_architectures":327,"interactions":0,"matches":81222,"pathways":67,"proteins":65500,"proteomes":21227,"sets":0,"structural_models":{"alphafold":56933,"bfvd":0},"structures":426,"taxa":61948},"entry_annotations":{"alignment:seed":752,"alignment:full":34674},"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"}}}