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Database: UniProt
Entry: G1CZN3_AGRST
LinkDB: G1CZN3_AGRST
Original site: G1CZN3_AGRST 
ID   G1CZN3_AGRST            Unreviewed;       420 AA.
AC   G1CZN3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE            EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
DE   Flags: Fragment;
GN   Name=atpB {ECO:0000313|EMBL:AEM37784.1};
OS   Agrostis stolonifera (Creeping bentgrass).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AEM37784.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Poeae Chloroplast Group 1 (Aveneae type);
OC   Agrostidodinae; Agrostidinae; Agrostis.
OX   NCBI_TaxID=63632 {ECO:0000313|EMBL:AEM37784.1};
RN   [1] {ECO:0000313|EMBL:AEM37784.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A11 {ECO:0000313|EMBL:AEM37784.1};
RX   PubMed=21809178; DOI=10.1007/s10265-011-0441-y;
RA   Lu J.M., Wen J., Lutz S., Wang Y.P., Li D.Z.;
RT   "Phylogenetic relationships of Chinese Adiantum based on five plastid
RT   markers.";
RL   J. Plant Res. 125:237-249(2012).
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. {ECO:0000256|ARBA:ARBA00037290}.
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:0000256|ARBA:ARBA00001741,
CC         ECO:0000256|RuleBase:RU003553};
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).
CC       {ECO:0000256|RuleBase:RU003553}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; JF935373; AEM37784.1; -; Genomic_DNA.
DR   AlphaFoldDB; G1CZN3; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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.
DR   CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR   CDD; cd01133; F1-ATPase_beta_CD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01039; atpD; 1.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW   ECO:0000256|RuleBase:RU003553};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW   Chloroplast {ECO:0000313|EMBL:AEM37784.1};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003553};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AEM37784.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          89..281
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEM37784.1"
SQ   SEQUENCE   420 AA;  45074 MW;  21449389CF60BE54 CRC64;
     AVAMSATDGL MRGMDAVDTG APLSVPVGET TLGRIFNVLG EPVDNLGPVQ NSATFPIHRS
     APAFTQLDTK LSIFETGIKV VDLLAPYRRG GKIGLFGGAG VGKTVLITES INNIAKAHGG
     VSVFGGVGER TREGNDLYME MKESKVINEQ NLSESKVALV YGQMNEPPGA RMRVGLTALT
     MAEYFRDINK RDVLLFIDNI FRFVQAGSEV SALLGRMPSA VGYQPTLGTE MGSLQERITS
     TKEGSITSIQ AVYVPADDLT DPAPATTFAH LDATTVLSRG LAAKGIYPAV DPLDSTSTML
     QPWIVGEEHY ETAQGVKQTL QRYKELQDII AILGLDELSE EDRLTVARAR KIERFLSQPF
     FVAEVFTGSP GKYVSLPETI KGFQMILPGE LDNLPEQAFY LVGNIDEAAA KAAALQAGGQ
//
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