{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,5]],"date-time":"2026-09-05T13:13:15Z","timestamp":1788613995701,"version":"build-2803163510"},"reference-count":30,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T00:00:00Z","timestamp":1793491200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP21H02627"],"award-info":[{"award-number":["JP21H02627"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP18K06661"],"award-info":[{"award-number":["JP18K06661"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP21K06546"],"award-info":[{"award-number":["JP21K06546"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP25K09957"],"award-info":[{"award-number":["JP25K09957"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Biochemistry and Biophysics"],"published-print":{"date-parts":[[2026,11]]},"DOI":"10.1016\/j.abb.2026.110983","type":"journal-article","created":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T06:49:09Z","timestamp":1787640549000},"page":"110983","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Functional discrepancy between F-type and A-type rotary ion-translocating ATPases in acid tolerance of Streptococcus anginosus"],"prefix":"10.1016","volume":"785","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4108-790X","authenticated-orcid":false,"given":"Mizuki","family":"Sekiya","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taichi","family":"Ishikawa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mayu","family":"Oyake","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Shimoyama","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Minoru","family":"Sasaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mayumi","family":"Nakanishi-Matsui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.abb.2026.110983_bib1","doi-asserted-by":"crossref","first-page":"3446","DOI":"10.1093\/gbe\/evw241","article-title":"Comparative genome analysis of the daptomycin-resistant Streptococcus anginosus strain J4206 associated with breakthrough bacteremia","volume":"8","author":"Rahman","year":"2016","journal-title":"Genome Biol. Evol."},{"key":"10.1016\/j.abb.2026.110983_bib2","doi-asserted-by":"crossref","DOI":"10.5812\/jjm.33863","article-title":"Intra-abdominal abscess and primary peritonitis caused by Streptococcus anginosus","volume":"9","author":"Terzi","year":"2016","journal-title":"Jundishapur J. Microbiol."},{"key":"10.1016\/j.abb.2026.110983_bib3","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1099\/00222615-43-6-405","article-title":"Potential pathogenic properties of members of the \"Streptococcus milleri\" group in relation to the production of endocarditis and abscesses","volume":"43","author":"Willcox","year":"1995","journal-title":"J. Med. Microbiol."},{"key":"10.1016\/j.abb.2026.110983_bib4","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1002\/cncr.33316","article-title":"Oral infectious bacteria in dental plaque and saliva as risk factors in patients with esophageal cancer","volume":"127","author":"Kawasaki","year":"2021","journal-title":"Cancer"},{"key":"10.1016\/j.abb.2026.110983_bib5","doi-asserted-by":"crossref","first-page":"174","DOI":"10.2323\/jgam.2017.11.005","article-title":"Aciduricity and acid tolerance mechanisms of Streptococcus anginosus","volume":"64","author":"Sasaki","year":"2018","journal-title":"J. Gen. Appl. Microbiol."},{"key":"10.1016\/j.abb.2026.110983_bib6","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1146\/annurev.biochem.66.1.717","article-title":"The ATP synthase--a splendid molecular machine","volume":"66","author":"Boyer","year":"1997","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.abb.2026.110983_bib7","doi-asserted-by":"crossref","first-page":"1711","DOI":"10.1016\/j.bbabio.2012.03.015","article-title":"Rotational catalysis in proton pumping ATPases: from E. coli F-ATPase to mammalian V-ATPase","volume":"1817","author":"Futai","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.abb.2026.110983_bib8","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1248\/bpb.b22-00396","article-title":"Proton pumping ATPases: rotational catalysis, physiological roles in oral pathogenic bacteria, and inhibitors","volume":"45","author":"Sekiya","year":"2022","journal-title":"Biol. Pharm. Bull."},{"key":"10.1016\/j.abb.2026.110983_bib9","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BST20110773","article-title":"The ATP synthase: the understood, the uncertain and the unknown","volume":"41","author":"Walker","year":"2013","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.abb.2026.110983_bib10","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/S1389-1723(01)80028-1","article-title":"Molecular biology of oxygen tolerance in lactic acid bacteria: functions of NADH oxidases and Dpr in oxidative stress","volume":"90","author":"Higuchi","year":"2000","journal-title":"J. Biosci. Bioeng."},{"key":"10.1016\/j.abb.2026.110983_bib11","doi-asserted-by":"crossref","DOI":"10.1093\/jambio\/lxad073","article-title":"F-type proton-pumping ATPase mediates acid tolerance in Streptococcus mutans","volume":"134","author":"Sekiya","year":"2023","journal-title":"J. Appl. Microbiol."},{"key":"10.1016\/j.abb.2026.110983_bib12","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.abb.2019.03.014","article-title":"Proton-pumping F-ATPase plays an important role in Streptococcus mutans under acidic conditions","volume":"666","author":"Sekiya","year":"2019","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.abb.2026.110983_bib13","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1016\/j.bbabio.2014.03.004","article-title":"ATP synthases from archaea: the beauty of a molecular motor","volume":"1837","author":"Gruber","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.abb.2026.110983_bib14","doi-asserted-by":"crossref","first-page":"10042","DOI":"10.1074\/jbc.271.17.10042","article-title":"The ntpJ gene in the Enterococcus hirae ntp operon encodes a component of KtrII potassium transport system functionally independent of vacuolar Na+-ATPase","volume":"271","author":"Murata","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2026.110983_bib15","doi-asserted-by":"crossref","first-page":"6556","DOI":"10.1128\/JB.181.20.6556-6559.1999","article-title":"A novel gene required for rhamnose-glucose polysaccharide synthesis in Streptococcus mutans","volume":"181","author":"Yamashita","year":"1999","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.abb.2026.110983_bib16","doi-asserted-by":"crossref","first-page":"3745","DOI":"10.1128\/iai.61.9.3745-3755.1993","article-title":"Construction of a model secretion system for oral streptococci","volume":"61","author":"Shiroza","year":"1993","journal-title":"Infect. Immun."},{"key":"10.1016\/j.abb.2026.110983_bib17","doi-asserted-by":"crossref","first-page":"8524","DOI":"10.1128\/JB.186.24.8524-8528.2004","article-title":"The F-ATPase operon promoter of Streptococcus mutans is transcriptionally regulated in response to external pH","volume":"186","author":"Kuhnert","year":"2004","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.abb.2026.110983_bib18","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/0147-619X(92)90044-B","article-title":"Molecular, genetic, and functional analysis of the basic replicon of pVA380-1, a plasmid of oral streptococcal origin","volume":"28","author":"LeBlanc","year":"1992","journal-title":"Plasmid"},{"key":"10.1016\/j.abb.2026.110983_bib19","doi-asserted-by":"crossref","first-page":"7070","DOI":"10.1016\/S0021-9258(19)62722-5","article-title":"Mutational replacements of conserved amino acid residues in the beta subunit resulted in defective assembly of H+-translocating ATPase (F0F1) in Escherichia coli","volume":"261","author":"Noumi","year":"1986","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2026.110983_bib20","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/j.bbrc.2013.12.025","article-title":"A unique F-type H+-ATPase from Streptococcus mutans: an active H+ pump at acidic pH","volume":"443","author":"Sasaki","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.abb.2026.110983_bib21","doi-asserted-by":"crossref","first-page":"18098","DOI":"10.1074\/jbc.M111567200","article-title":"A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification","volume":"277","author":"Sun-Wada","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2026.110983_bib22","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1126\/science.1106753","article-title":"A diarylquinoline drug active on the ATP synthase of\u00a0Mycobacterium tuberculosis","volume":"307","author":"Andries","year":"2005","journal-title":"Science"},{"key":"10.1016\/j.abb.2026.110983_bib23","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1016\/j.bbrc.2018.03.066","article-title":"Porphyromonas gingivalis is highly sensitive to inhibitors of a proton-pumping ATPase","volume":"498","author":"Sekiya","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.abb.2026.110983_bib24","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.bbabio.2014.07.020","article-title":"Infrared spectroscopic studies on the V-ATPase","volume":"1847","author":"Kandori","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.abb.2026.110983_bib25","article-title":"ProAD - a database of rotary ion-translocating ATPases in prokaryotic genomes","volume":"11","author":"Litvin","year":"2024","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.abb.2026.110983_bib26","doi-asserted-by":"crossref","first-page":"11945","DOI":"10.1073\/pnas.0711697105","article-title":"The protonmotive force is required for maintaining ATP homeostasis and viability of hypoxic, nonreplicating Mycobacterium tuberculosis","volume":"105","author":"Rao","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.abb.2026.110983_bib27","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.ijbiomac.2014.06.055","article-title":"Strong inhibitory effects of curcumin and its demethoxy analog on Escherichia coli ATP synthase F1 sector","volume":"70","author":"Sekiya","year":"2014","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.abb.2026.110983_bib28","doi-asserted-by":"crossref","first-page":"22771","DOI":"10.1074\/jbc.M112.374868","article-title":"Binding of phytopolyphenol piceatannol disrupts \u03b2\/\u03b3 subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATPase","volume":"287","author":"Sekiya","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.abb.2026.110983_bib29","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1021\/mp700113r","article-title":"Bioavailability of curcumin: problems and promises","volume":"4","author":"Anand","year":"2007","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.abb.2026.110983_bib30","doi-asserted-by":"crossref","first-page":"2541","DOI":"10.1021\/jf404694y","article-title":"Absorption and metabolism of piceatannol in rats","volume":"62","author":"Setoguchi","year":"2014","journal-title":"J. Agric. Food Chem."}],"container-title":["Archives of Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986126002559?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986126002559?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,5]],"date-time":"2026-09-05T12:43:25Z","timestamp":1788612205000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003986126002559"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,11]]},"references-count":30,"alternative-id":["S0003986126002559"],"URL":"https:\/\/doi.org\/10.1016\/j.abb.2026.110983","relation":{},"ISSN":["0003-9861"],"issn-type":[{"value":"0003-9861","type":"print"}],"subject":[],"published":{"date-parts":[[2026,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Functional discrepancy between F-type and A-type rotary ion-translocating ATPases in acid tolerance of Streptococcus anginosus","name":"articletitle","label":"Article Title"},{"value":"Archives of Biochemistry and Biophysics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.abb.2026.110983","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"110983"}}