{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q21ZA0","uniProtkbId":"ATPF2_ALBFT","entryAudit":{"firstPublicDate":"2009-04-14","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-04-18","entryVersion":99,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)","commonName":"Rhodoferax ferrireducens","taxonId":338969,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Comamonadaceae","Rhodoferax"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"ATP synthase subunit b 2"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"ATP synthase F(0) sector subunit b 2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"ATPase subunit I 2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"F-type ATPase subunit b 2"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"F-ATPase subunit b 2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"atpF2"},"orderedLocusNames":[{"value":"Rfer_1167"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases 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. 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"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01398"}],"value":"Belongs to the ATPase B chain family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"ATP synthase subunit b 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