ID   ATPB_BRACM              Reviewed;          32 AA.
AC   P83505;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=ATP synthase subunit beta, chloroplastic;
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 sector subunit beta;
DE   AltName: Full=F-ATPase subunit beta;
DE   Flags: Fragments;
GN   Name=atpB;
OS   Brassica campestris (Field mustard).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711;
RN   [1]
RP   PROTEIN SEQUENCE, BLOCKAGE OF N-TERMINUS, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RC   TISSUE=Leaf mesophyll;
RX   PubMed=15694282; DOI=10.1016/j.plaphy.2004.11.001;
RA   Jiao S., Hilaire E., Guikema J.A.;
RT   "Identification and differential accumulation of two isoforms of the CF1-
RT   beta subunit under high light stress in Brassica rapa.";
RL   Plant Physiol. Biochem. 42:883-890(2004).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The catalytic sites are hosted primarily by the
CC       beta subunits (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10106};
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main
CC       subunits: a(1), b(1), b'(1) and c(9-12) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: The 56 kDa isoform is not detected in etiolated
CC       cotyledons The 54 kDa isoform exists even in the dark and increases
CC       very rapidly for 96 hours upon illumination.
CC       {ECO:0000269|PubMed:15694282}.
CC   -!- INDUCTION: The 56 kDa isoform is constitutively expressed. The 54 kDa
CC       isoform increases 9-fold during 10 hours of high light stress and
CC       decreases after 24 hours of photoinhibitory treatment.
CC       {ECO:0000269|PubMed:15694282}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: Two isoforms of 54 and 56 kDa with the same peptide
CC       fingerprint are found in the chloroplast. The synthesis of the major 56
CC       kDa isoform is coupled to the assembly into the thylakoid membrane,
CC       while the 54 kDa isoform accumulates in response to various light
CC       stress conditions.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83505; -.
DR   SMR; P83505; -.
DR   STRING; 3711.Bra006013.1-P; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); 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-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; CF(1); Chloroplast; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Plastid; Thylakoid; Translocase; Transport.
FT   CHAIN           <1..>32
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000144501"
FT   NON_CONS        21..22
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         32
SQ   SEQUENCE   32 AA;  3403 MW;  78C5671FDAD4A7C8 CRC64;
     KDALVYGQMN EPPGARMRVG LKDGSITSIQ AV