ID Q09R88_9BRYO Unreviewed; 472 AA.
AC Q09R88;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
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:ABI48177.1};
OS Thamnobryum alleghaniense.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ABI48177.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Bryidae; Hypnanae; Hypnales; Neckeraceae;
OC Thamnobryum.
OX NCBI_TaxID=94559 {ECO:0000313|EMBL:ABI48177.1};
RN [1] {ECO:0000313|EMBL:ABI48177.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17030812; DOI=10.1073/pnas.0603335103;
RA Qiu Y.L., Li L., Wang B., Chen Z., Knoop V., Groth-Malonek M.,
RA Dombrovska O., Lee J., Kent L., Rest J., Estabrook G.F., Hendry T.A.,
RA Taylor D.W., Testa C.M., Ambros M., Crandall-Stotler B., Duff R.J.,
RA Stech M., Frey W., Quandt D., Davis C.C.;
RT "The deepest divergences in land plants inferred from phylogenomic
RT evidence.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15511-15516(2006).
RN [2] {ECO:0000313|EMBL:ABI48177.1}
RP NUCLEOTIDE SEQUENCE.
RA Qiu Y.-L., Li L., Wang B., Chen Z., Knoop V., Groth-Malonek M.,
RA Dombrovska O., Lee J., Kent L., Rest J., Estabrook G.F., Hendry T.A.,
RA Taylor D.W., Testa C.M., Ambros M., Crandall-Stotler B., Duff R.Joel.,
RA Stech M., Frey W., Quandt D., Davis C.C.;
RL Submitted (MAY-2006) 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; DQ646080; ABI48177.1; -; Genomic_DNA.
DR AlphaFoldDB; Q09R88; -.
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:ABI48177.1};
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:ABI48177.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 142..334
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABI48177.1"
SQ SEQUENCE 472 AA; 50834 MW; 41E43A8C40875F0F CRC64;
ITQIIGPVLD VTSSPGKMPN IYNSLIVEGQ NTAGQEINVT CEVQQLLGNN KVRAVAMSAT
DGLMRGMQVI DTGAPLSVPV GEATLGRIFN VLGETVDNLG PVDASTTFPI HRSAPAFTQL
DTKLSIFETG IKVVDLSAPY RRGGKIGLFG GAGVGKTVLI MELINNIAKA HGGVSVFGGV
GERTREGNDL YMEMKESKVI NEENISESKV ALVYGQTNEP PGARMRVGLT ALTMAEYFRD
VNKQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL STEMGTLQER ITSTKEGSIT
SIQAVYVPAD DLTDPAPATT FAHLDATTVL SRGLAAKGIY PAVDPSDSTS TMLQPWIVGE
EHYETAQGVK QTLQRYKELQ DIIAILGLDE LSEEDRLTVA RARKIERFLS QPFFVAEVFT
GSPGKYVSLI ETIKGFQMIL SGELDSFPEQ AFYLVGNIDE ATAKAATLQV EN
//
