ATPF_SPIOL
ID ATPF_SPIOL Reviewed; 184 AA.
AC P06453;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 115.
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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
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 [GENOMIC DNA].
RA Hennig J., Herrmann R.G.;
RT "Chloroplast ATP synthase of spinach contains nine nonidentical subunit
RT species, six of which are encoded by plastid chromosomes in two operons in
RT a phylogenetically conserved arrangement.";
RL Mol. Gen. Genet. 203:117-128(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2443718; DOI=10.1016/0022-2836(87)90690-5;
RA Hudson G.S., Mason J.G., Holton T.A., Koller B., Cox G.B., Whitfeld P.R.,
RA Bottomley W.;
RT "A gene cluster in the spinach and pea chloroplast genomes encoding one CF1
RT and three CF0 subunits of the H+-ATP synthase complex and the ribosomal
RT protein S2.";
RL J. Mol. Biol. 196:283-298(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
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; X03775; CAA27404.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88711.1; -; Genomic_DNA.
DR PIR; S00583; PWSP1.
DR RefSeq; NP_054918.1; NC_002202.1.
DR PDB; 6FKF; EM; 3.10 A; b=1-184.
DR PDB; 6FKH; EM; 4.20 A; b=1-184.
DR PDB; 6FKI; EM; 4.30 A; b=1-184.
DR PDB; 6VM1; EM; 7.90 A; I=1-184.
DR PDB; 6VM4; EM; 7.08 A; I=1-184.
DR PDB; 6VMB; EM; 5.23 A; I=1-184.
DR PDB; 6VMG; EM; 6.46 A; I=1-184.
DR PDB; 6VOF; EM; 4.51 A; I=1-184.
DR PDB; 6VOH; EM; 4.16 A; I=1-184.
DR PDB; 6VOJ; EM; 4.34 A; I=1-184.
DR PDB; 6VOL; EM; 4.06 A; I=1-184.
DR PDB; 6VON; EM; 3.35 A; I=1-184.
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; P06453; -.
DR SMR; P06453; -.
DR IntAct; P06453; 1.
DR STRING; 3562.P06453; -.
DR ChEMBL; CHEMBL2366567; -.
DR PRIDE; P06453; -.
DR GeneID; 2715578; -.
DR KEGG; soe:2715578; -.
DR OrthoDB; 1333093at2759; -.
DR PRO; PR:P06453; -.
DR Proteomes; UP000054095; Chloroplast.
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: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 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; CF(0); Chloroplast;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Plastid; Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..184
FT /note="ATP synthase subunit b, chloroplastic"
FT /id="PRO_0000082423"
FT TRANSMEM 27..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT HELIX 31..156
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 161..181
FT /evidence="ECO:0007829|PDB:6FKF"
SQ SEQUENCE 184 AA; 20990 MW; 606C9CFF31A9DD03 CRC64;
MKNVTDSFVF LGHWPSAGSF GFNTDILATN LINLSVVLGV LIFFGKGVLS DLLDNRKQRI
LNTIRNSEEL RGKAIEQLEK ARARLKKVEM DADQFRVNGY SEIEREKMNL INSTYKTLEQ
FENYKNETIQ FEQQKAINQV RQRVFQQALQ GALGTLNSCL NNELHLRTIN ANIGMFGAMN
EITD
