ATPF2_SPIOL
ID ATPF2_SPIOL Reviewed; 222 AA.
AC P31853; P32981;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=ATP synthase subunit b', chloroplastic;
DE AltName: Full=ATP synthase F(0) sector subunit b';
DE AltName: Full=ATPase subunit II;
DE Flags: Precursor;
GN Name=ATPF2 {ECO:0000305}; Synonyms=ATPG;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Monatol; TISSUE=Seedling;
RX PubMed=8325369; DOI=10.1016/0014-5793(93)81789-3;
RA Herrmann R.G., Steppuhn J., Herrmann G.S., Nelson N.;
RT "The nuclear-encoded polypeptide Cfo-II from spinach is a real, ninth
RT subunit of chloroplast ATP synthase.";
RL FEBS Lett. 326:192-198(1993).
RN [2]
RP PROTEIN SEQUENCE OF 76-107.
RA Berzborn R.J., Otto J., Finke W., Meyer H.E., Block J.;
RT "Conclusions from N-terminal amino acid sequences of subunits delta from
RT spinach and maize CF-1 and of subunits I and II from spinach CF-0.";
RL Biol. Chem. Hoppe-Seyler 368:551-552(1987).
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 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged
CC and duplicated form of b found in plants and photosynthetic bacteria
CC (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-
CC pass membrane protein.
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:0000305}.
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DR EMBL; X71397; CAA50520.1; -; mRNA.
DR PIR; S34473; S34473.
DR PDB; 6FKF; EM; 3.10 A; p=1-222.
DR PDB; 6FKH; EM; 4.20 A; p=1-222.
DR PDB; 6FKI; EM; 4.30 A; p=1-222.
DR PDB; 6VM1; EM; 7.90 A; J=1-222.
DR PDB; 6VM4; EM; 7.08 A; J=1-222.
DR PDB; 6VMB; EM; 5.23 A; J=1-222.
DR PDB; 6VMG; EM; 6.46 A; J=1-222.
DR PDB; 6VOF; EM; 4.51 A; J=1-222.
DR PDB; 6VOH; EM; 4.16 A; J=1-222.
DR PDB; 6VOJ; EM; 4.34 A; J=1-222.
DR PDB; 6VOL; EM; 4.06 A; J=1-222.
DR PDB; 6VON; EM; 3.35 A; J=1-222.
DR PDBsum; 6FKF; -.
DR PDBsum; 6FKH; -.
DR PDBsum; 6FKI; -.
DR PDBsum; 6VM1; -.
DR PDBsum; 6VM4; -.
DR PDBsum; 6VMB; -.
DR PDBsum; 6VMG; -.
DR PDBsum; 6VOF; -.
DR PDBsum; 6VOH; -.
DR PDBsum; 6VOJ; -.
DR PDBsum; 6VOL; -.
DR PDBsum; 6VON; -.
DR AlphaFoldDB; P31853; -.
DR SMR; P31853; -.
DR IntAct; P31853; 1.
DR ChEMBL; CHEMBL2366567; -.
DR OrthoDB; 1604952at2759; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR HAMAP; MF_01399; ATP_synth_bprime; 1.
DR InterPro; IPR034679; ATP_synth_b.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR Pfam; PF00430; ATP-synt_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; CF(0); Chloroplast; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Plastid; Thylakoid; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 76..222
FT /note="ATP synthase subunit b', chloroplastic"
FT /id="PRO_0000002635"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 79
FT /note="E -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 89..107
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 109..201
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:6FKF"
SQ SEQUENCE 222 AA; 24460 MW; 8664CAEA810A5ED1 CRC64;
MANMLVASSS KTLPTTTTTT ITPKPKFPLL KTPLLKLSPP QLPPLKHLNL SVLKSAAITA
TPLTLSFLLP YPSLAEEIEK ASLFDFNLTL PIIMAEFLFL MFALDKIYYT PLGDFMDKRD
ASIKEQLSGV KDTSSEVKQL EEQANAVMRA ARAEISAALN KMKKETQLEV EAKLAEGRKK
IEVELQEALG SLEQQKEDTI KSLDSQISAL SDDIVKKVLP VS
