ID A0A9E7VAT0_9LILI Unreviewed; 187 AA. AC A0A9E7VAT0; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 27-NOV-2024, entry version 5. DE RecName: Full=ATP synthase subunit b, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01398}; DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000256|HAMAP-Rule:MF_01398}; DE AltName: Full=ATPase subunit I {ECO:0000256|HAMAP-Rule:MF_01398}; GN Name=atpF {ECO:0000256|HAMAP-Rule:MF_01398, GN ECO:0000313|EMBL:UZC33398.1}; OS Vallisneria denseserrulata x Vallisneria spiralis. OG Plastid; Chloroplast {ECO:0000313|EMBL:UZC33398.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Hydrocharitaceae; Vallisneria. OX NCBI_TaxID=1552891 {ECO:0000313|EMBL:UZC33398.1}; RN [1] {ECO:0000313|EMBL:UZC33398.1} RP NUCLEOTIDE SEQUENCE. RA Gao Y.; RT "Complete chloroplast of Vallisneria spiralis."; RL Submitted (FEB-2022) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the F(0) channel, it forms part of the CC peripheral stalk, linking F(1) to F(0). {ECO:0000256|HAMAP- CC Rule:MF_01398}. CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence CC of a proton or sodium gradient. F-type ATPases consist of two CC structural domains, F(1) containing the extramembraneous catalytic core CC and F(0) containing the membrane proton channel, linked together by a CC central stalk and a peripheral stalk. During catalysis, ATP synthesis CC in the catalytic domain of F(1) is coupled via a rotary mechanism of CC the central stalk subunits to proton translocation. CC {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-Rule:MF_01398}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core CC - and F(0) - the membrane proton channel. F(1) has five subunits: CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main CC subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains CC form an alternating ring which encloses part of the gamma chain. F(1) CC is attached to F(0) by a central stalk formed by the gamma and epsilon CC chains, while a peripheral stalk is formed by the delta, b and b' CC chains. {ECO:0000256|HAMAP-Rule:MF_01398}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01398}; CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01398}. CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as CC CF(1)CF(0). {ECO:0000256|HAMAP-Rule:MF_01398}. CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000256|HAMAP- CC Rule:MF_01398, ECO:0000256|RuleBase:RU003848}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; OM630415; UZC33398.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule. DR CDD; cd06503; ATP-synt_Fo_b; 1. DR HAMAP; MF_01398; ATP_synth_b_bprime; 1. DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt. DR PANTHER; PTHR34264; ATP SYNTHASE SUBUNIT B, CHLOROPLASTIC; 1. DR PANTHER; PTHR34264:SF3; ATP SYNTHASE SUBUNIT B, CHLOROPLASTIC; 1. DR Pfam; PF00430; ATP-synt_B; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP- KW Rule:MF_01398}; KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01398}; KW Chloroplast {ECO:0000313|EMBL:UZC33398.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01398}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_01398}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01398}; KW Plastid {ECO:0000313|EMBL:UZC33398.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01398}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01398}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01398}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01398}. FT COILED 65..99 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 187 AA; 21381 MW; 9C43E64FC400B2D7 CRC64; MKNLSDSFLS LVDYWPSAGS FGLNTDILAT NPINLSVVLG VLISFGKGVL TDLLDNRKQR ILSILRNSEE LRRSAVEELE KARDRLRKVE READEYRVNG YSEIEREKAN LIHATSDSLE QLESSKKETL RFEQQRAINQ VRQRVFQQAL ERAMETLTHC LNSESELHFR TISANIGILG TMEEITN //