ATPF_NANDO
ID ATPF_NANDO Reviewed; 184 AA.
AC Q09FX5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=ATP synthase subunit b, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398};
OS Nandina domestica (Heavenly bamboo).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Nandinoideae;
OC Nandina.
OX NCBI_TaxID=41776;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16934154; DOI=10.1186/1471-2229-6-17;
RA Moore M.J., Dhingra A., Soltis P.S., Shaw R., Farmerie W.G., Folta K.M.,
RA Soltis D.E.;
RT "Rapid and accurate pyrosequencing of angiosperm plastid genomes.";
RL BMC Plant Biol. 6:17-17(2006).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01398}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC CF(1)CF(0).
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; DQ923117; ABI49849.1; -; Genomic_DNA.
DR RefSeq; YP_740636.1; NC_008336.1.
DR AlphaFoldDB; Q09FX5; -.
DR SMR; Q09FX5; -.
DR GeneID; 4271566; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR Pfam; PF00430; ATP-synt_B; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Chloroplast; Hydrogen ion transport; Ion transport;
KW Membrane; Plastid; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..184
FT /note="ATP synthase subunit b, chloroplastic"
FT /id="PRO_0000368953"
FT TRANSMEM 27..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ SEQUENCE 184 AA; 20950 MW; 20356A1A101B7604 CRC64;
MKNVTDSFVS LGHWPSAGSF GFNTDILATN PINLSVVLGV LIFFGKGVLS DLLDNRKQRI
LNTIRNSEEL REGAIERLEK ARARLRKVEK EAEDYIVNGY QEIEREKLNL RNSIGKNLER
LENYKNETIQ FEQQRAINQV RQRVFQQALQ GALGTLNSCL NNELHLRTIS ANIGMFGAMK
EITD