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Database: UniProt
Entry: A0A1L6Z637_CAPCH
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ID   A0A1L6Z637_CAPCH        Unreviewed;       498 AA.
AC   A0A1L6Z637;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
GN   Name=atpB {ECO:0000256|HAMAP-Rule:MF_01347,
GN   ECO:0000313|EMBL:APT41729.1};
GN   ORFNames=C329_p061 {ECO:0000313|EMBL:ANJ03964.1};
OS   Capsicum chinense (Scotch bonnet) (Bonnet pepper).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:APT41729.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=80379 {ECO:0000313|EMBL:APT41729.1};
RN   [1] {ECO:0000313|EMBL:ANJ03964.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Park H.-S., Lee J., Lee S.-C., Yang T.-J., Yoon J.B.;
RT   "The complete chloroplast genome sequence of Capsicum chinenese Jacp.
RT   (Solanaceae).";
RL   Mitochondrial DNA Part B Resour 0:0-0(2016).
RN   [2] {ECO:0000313|EMBL:APT41729.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Lee G.-A., Chung J.-W., Ma K.-H., Raveendar S.;
RT   "Complete chloroplast genome sequence of five Capsicum species.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AYN59637.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30336638;
RA   D'Agostino N., Tamburino R., Cantarella C., De Carluccio V., Sannino L.,
RA   Cozzolino S., Cardi T., Scotti N.;
RT   "The Complete Plastome Sequences of Eleven Capsicum Genotypes: Insights
RT   into DNA Variation and Molecular Evolution.";
RL   Genes (Basel) 9:E503-E503(2018).
RN   [4] {ECO:0000313|EMBL:QYJ55353.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Arbizu C., Saldana C., Ferro-Mauricio R., Chavez-Galarza J., Contreras S.,
RA   Guerrero-Abad J.C., Maicelo-Quintana J.;
RT   "Characterization of the complete chloroplast genome of a Peruvian landrace
RT   of Capsicum chinense Jacq. (Solanaceae), arnaucho chile pepper.";
RL   Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_01347}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01347, 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). {ECO:0000256|HAMAP-
CC       Rule:MF_01347, ECO:0000256|RuleBase:RU003553}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01347}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01347}.
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DR   EMBL; KU041709; ANJ03964.1; -; Genomic_DNA.
DR   EMBL; KX913217; APT41729.1; -; Genomic_DNA.
DR   EMBL; MH559321; AYN59637.1; -; Genomic_DNA.
DR   EMBL; MZ379791; QYJ55353.1; -; Genomic_DNA.
DR   RefSeq; YP_009262870.1; NC_030543.1.
DR   STRING; 80379.A0A1L6Z637; -.
DR   GeneID; 32984160; -.
DR   OrthoDB; 3420200at2759; -.
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-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
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; cd18115; ATP-synt_F1_beta_N; 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; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
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   Pfam; PF02874; ATP-synt_ab_N; 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, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347};
KW   Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:APT41729.1};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:APT41729.1};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}.
FT   DOMAIN          164..356
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   498 AA;  53599 MW;  8826C6DDFC37EFEE CRC64;
     MRINPTTSGS GVSTLEKKNL GRVVQIIGPV LDVAFPPGKM PNIYNALVVQ GRDSVDQPIN
     VACEVQQLLG NNRVRAVAMS ATDGLTRGME VIDTGAPISV PVGGATLGRI FNVLGEPVDN
     LGPVDTSTTS PIHRSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
     LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEENIAES KVALVYGQMN
     EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP
     TLSTEMGSLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG
     IYPAVDPLDS TSTMLQPRIV GEEHYETAQR VKQTLQRYKE LQDIIAILGL DELSEEDRLL
     VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFQL ILSGELDGLP EQAFYLVGNI
     DEATAKAMNL EMESNLKK
//
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