{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"B5FVB3","uniProtkbId":"ATP19_YARLI","entryAudit":{"firstPublicDate":"2018-10-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-10-14","entryVersion":66,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Yarrowia lipolytica (strain CLIB 122 / E 150)","commonName":"Yeast","synonyms":["Candida lipolytica"],"taxonId":284591,"evidences":[{"evidenceCode":"ECO:0000312","source":"Proteomes","id":"UP000001300"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Dipodascomycetes","Dipodascales","Dipodascales incertae sedis","Yarrowia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P81451"}],"value":"ATP synthase subunit K, mitochondrial"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P81451"}],"value":"ATP19"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"CAR64284.1"}],"value":"YALI0_B11913g"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25759169"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27373333"}],"value":"Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27373333). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (PubMed:27373333). Part of the complex F(0) domain (PubMed:27373333). Minor subunit located with subunit a/ATP6 in the membrane (PubMed:27373333). The K/ATP19 chain binds the dimeric form by interacting with the G/ATP20 and E/TIM11 chains (PubMed:27373333)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25759169"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27373333"}],"value":"F-type ATP synthases have 2 components, the catalytic core F(1) and the membrane-embedded component F(0), linked together by a central stalk and a peripheral stalk (PubMed:27373333). The central stalk, also called rotor shaft, is often seen as part of F(1) (PubMed:27373333). The peripheral stalk is seen as part of F(0) (PubMed:27373333). F(0) contains the membrane channel next to the rotor (PubMed:27373333). F-type ATP synthases form dimers but each monomer functions independently in ATP generation (PubMed:27373333). The dimer consists of 17 different polypeptides: ATP1 (subunit alpha, 3 molecules per monomer, part of F(1)), ATP2 (subunit beta, 3 copies per monomer, part of F(1)), ATP3 (subunit gamma, part of the central stalk), ATP4 (subunit b, part of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP, part of the peripheral stalk), ATP6 (subunit a, part of the peripheral stalk), ATP7 (subunit d, part of the peripheral stalk), ATP8 (subunit 8, part of the peripheral stalk), OLI1 (subunit c, part of the rotor, 10 molecules per monomer), ATP14 (subunit h, part of the peripheral stalk), ATP15 (subunit epsilon, part of the central stalk), ATP16 (subunit delta, part of the central stalk), ATP17 (subunit f, part of the peripheral stalk), ATP18 (subunit i/j, part of the peripheral stalk), ATP19 (subunit k, dimer-specific, at interface between monomers), ATP20 (subunit g, at interface between monomers), TIM11 (subunit e, at interface between monomers) (PubMed:25759169, PubMed:27373333)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27373333"}],"value":"The F-type ATP synthase complex is anchored in the mitochondrial inner membrane via the F(0) domain with the F(1) domain and the peripheral stalk extending into the mitochondrial matrix"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25759169"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the ATP19 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"ATP synthase subunit K, mitochondrial","evidences":[{"evidenceCode":"ECO:0000305"}],"featureId":"PRO_0000445306"},{"type":"Transmembrane","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}],"keywords":[{"id":"KW-0066","category":"Biological process","name":"ATP synthesis"},{"id":"KW-0138","category":"Cellular component","name":"CF(0)"},{"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"15229592","citationType":"journal article","authors":["Dujon B.","Sherman D.","Fischer G.","Durrens P.","Casaregola S.","Lafontaine I.","de Montigny J.","Marck C.","Neuveglise C.","Talla E.","Goffard N.","Frangeul L.","Aigle M.","Anthouard V.","Babour A.","Barbe V.","Barnay S.","Blanchin S.","Beckerich J.-M.","Beyne E.","Bleykasten C.","Boisrame A.","Boyer J.","Cattolico L.","Confanioleri F.","de Daruvar A.","Despons L.","Fabre E.","Fairhead C.","Ferry-Dumazet H.","Groppi A.","Hantraye F.","Hennequin C.","Jauniaux N.","Joyet P.","Kachouri R.","Kerrest A.","Koszul R.","Lemaire M.","Lesur I.","Ma L.","Muller H.","Nicaud J.-M.","Nikolski M.","Oztas S.","Ozier-Kalogeropoulos O.","Pellenz S.","Potier S.","Richard G.-F.","Straub M.-L.","Suleau A.","Swennen D.","Tekaia F.","Wesolowski-Louvel M.","Westhof E.","Wirth B.","Zeniou-Meyer M.","Zivanovic Y.","Bolotin-Fukuhara M.","Thierry A.","Bouchier C.","Caudron B.","Scarpelli C.","Gaillardin C.","Weissenbach J.","Wincker P.","Souciet J.-L."],"citationCrossReferences":[{"database":"PubMed","id":"15229592"},{"database":"DOI","id":"10.1038/nature02579"}],"title":"Genome evolution in yeasts.","publicationDate":"2004","journal":"Nature","firstPage":"35","lastPage":"44","volume":"430"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"CLIB 122 / E 150","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000312","source":"Proteomes","id":"UP000001300"}]},{"referenceNumber":2,"citation":{"id":"25759169","citationType":"journal article","authors":["Liu S.","Charlesworth T.J.","Bason J.V.","Montgomery M.G.","Harbour M.E.","Fearnley I.M.","Walker J.E."],"citationCrossReferences":[{"database":"PubMed","id":"25759169"},{"database":"DOI","id":"10.1042/bj20150197"}],"title":"The purification and characterization of ATP synthase complexes from the mitochondria of four fungal species.","publicationDate":"2015","journal":"Biochem. 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