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Database: UniProt
Entry: H2BPC7_9MONI
LinkDB: H2BPC7_9MONI
Original site: H2BPC7_9MONI 
ID   H2BPC7_9MONI            Unreviewed;       427 AA.
AC   H2BPC7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-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:AEY64260.1};
OS   Nephrolepis davallioides.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AEY64260.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Polypodiineae;
OC   Nephrolepidaceae; Nephrolepis.
OX   NCBI_TaxID=910274 {ECO:0000313|EMBL:AEY64260.1};
RN   [1] {ECO:0000313|EMBL:AEY64260.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22223449; DOI=10.1093/sysbio/sys001;
RA   Rothfels C.J., Larsson A., Kuo L.Y., Korall P., Chiou W.L., Pryer K.M.;
RT   "Overcoming deep roots, fast rates, and short internodes to resolve the
RT   ancient rapid radiation of eupolypod II ferns.";
RL   Syst. Biol. 61:490-509(2012).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000256|RuleBase:RU003553}.
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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; JF832172; AEY64260.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2BPC7; -.
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; 2.40.10.170; -; 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; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
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; SSF50615; N-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:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:AEY64260.1};
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:AEY64260.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          96..288
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEY64260.1"
FT   NON_TER         427
FT                   /evidence="ECO:0000313|EMBL:AEY64260.1"
SQ   SEQUENCE   427 AA;  45935 MW;  F84FEAF3E9390010 CRC64;
     LGNNEVRAVA MSATDGLMRG MGAVDTGAPL SVPVGETTLG RIFNVLGEPV DNLGPVQSST
     TFPIHRSAPA FTQLDTKLSI FETGIKVVDL LAPYRRGGKI GLFGGAGVGK TVLIMELINN
     IAKAHGGVSV FGGVGERTRE GNDLYMEMKE SKVINEQNIS ESKVALVYGQ MNEPPGARMR
     VGLTALTMAE YFRDVNKQDV LLFIDNIFRF VQAGSEVSAL LGRMPSAVGY QPTLGTEMGS
     LQERITSTKE GSITSIQAVY VPADDLTDPA PATTSAHLDA TTVLSRGLAA KGIYPAVDPL
     DSTSTMLQPW IVGEEHYETA QGVKQTLQRY KELQDIIAIL GLDELSEEDR LTVARARKIE
     RFLSQPFFVA EVFTGSPGKY VRLSETIKGF KMILSGELDN IPEQAFYLVG NIDEATAKAA
     ALQVEGQ
//
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