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Database: UniProt
Entry: M1HIH1_9ASTR
LinkDB: M1HIH1_9ASTR
Original site: M1HIH1_9ASTR 
ID   M1HIH1_9ASTR            Unreviewed;       467 AA.
AC   M1HIH1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
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:AGE45926.1};
OS   Adenophora stricta.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AGE45926.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Campanulaceae; Adenophora.
OX   NCBI_TaxID=82279 {ECO:0000313|EMBL:AGE45926.1};
RN   [1] {ECO:0000313|EMBL:AGE45926.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kim K.-A., Yoo K.-O.;
RT   "Phylogenetic Relationships of Korean Campanulaceae Based on Eight regions
RT   sequences in Chloroplast DNA.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ATV94850.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kim H.-J., Son D.-C., Joo M., Choi K., Shin C.-H., Kang S.-H.;
RT   "The chemotaxonomic classification of Korean Campanulaceae and its
RT   correlation with molecular phylogeny.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; KC146436; AGE45926.1; -; Genomic_DNA.
DR   EMBL; KY368967; ATV94850.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1HIH1; -.
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; 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,
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:AGE45926.1};
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}; Plastid {ECO:0000313|EMBL:AGE45926.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          144..336
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGE45926.1"
FT   NON_TER         467
FT                   /evidence="ECO:0000313|EMBL:AGE45926.1"
SQ   SEQUENCE   467 AA;  50317 MW;  967E767DC9E8549D CRC64;
     GRIGQIIGPV LDVAFPAGKM PNIYNALVVK GRDTLGQPIN VTCEVQQLLG NNRVRAVAMS
     ATDGLMRGME VIDTGTPLSV PVGGATLGRI FNVLGEPIDN LGPVDTRTTS PIHRSAPAFI
     DLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA KAHGGVSVFG
     GVGERTREGN DLYKEMKDSG VINEQKFAES KVALVYGQMN EPPGARMRVG LTALTMAEYF
     RDVNKQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLSTEMGSLQ ERITSTKKGS
     ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG IYPAVDPLDS TSTMLQPRIV
     SDEHYKTAQS VKQTLQRYKE LQDIITILGL DELSEEDRLT VARARKIERF LSQPFFVAEV
     FTGSTGKYVG LVETIRGFQL ILSGKFDGLP EQAFYMVGNI DEATAKA
//
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