ID Q42139_ARATH Unreviewed; 219 AA.
AC Q42139;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 2.
DT 24-JAN-2024, entry version 177.
DE SubName: Full=AT4g32260/F10M6_100 {ECO:0000313|EMBL:AAL24209.1};
DE SubName: Full=ATP synthase beta chain (Subunit II) {ECO:0000313|EMBL:CAB52473.1};
DE EC=3.6.1.34 {ECO:0000313|EMBL:CAB52473.1};
DE SubName: Full=ATPase, F0 complex, subunit B/B', bacterial/chloroplast {ECO:0000313|EMBL:AEE86027.1};
DE SubName: Full=H+-transporting ATP synthase chain 9-like protein {ECO:0000313|EMBL:AAM63254.1};
DE SubName: Full=H+-transporting ATP synthase chain9 - like protein {ECO:0000313|EMBL:CAA16964.1};
GN Name=PDE334 {ECO:0000313|EMBL:AEE86027.1, ECO:0000313|TAIR:AT4G32260};
GN Synonyms=atpG {ECO:0000313|EMBL:CAB52473.1}, PIGMENT DEFECTIVE 334
GN {ECO:0000313|EMBL:AEE86027.1};
GN OrderedLocusNames=At4g32260 {ECO:0000313|Araport:AT4G32260,
GN ECO:0000313|EMBL:AEE86027.1};
GN ORFNames=F10M6.100 {ECO:0000313|EMBL:CAA16964.1}, F10M6_100
GN {ECO:0000313|EMBL:AEE86027.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:CAA16964.1};
RN [1] {ECO:0000313|EMBL:CAB52473.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=7846151; DOI=10.1104/pp.106.4.1241;
RA Newman T., de Bruijn F.J., Green P., Keegstra K., Kende H., Mclntosh L.,
RA Ohlrogge J., Raikhel N., Somerville S., Thomashow M., Retzel E.,
RA Somerville C.;
RT "Genes galore: a summary of methods for accessing results from large-scale
RT partial sequencing of anonymous Arabidopsis cDNA clones.";
RL Plant Physiol. 106:1241-1255(1994).
RN [2] {ECO:0000313|EMBL:CAA16964.1}
RP NUCLEOTIDE SEQUENCE.
RA EU Arabidopsis sequencing project;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAA16964.1}
RP NUCLEOTIDE SEQUENCE.
RA Bevan M., Weichselgartner M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Hoheisel J., Mewes H.W., Mayer K., Schueller C.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AEE86027.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=10617198; DOI=10.1038/47134;
RG EU;
RG CSHL and WU Arabidopsis Sequencing Project;
RA Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Kotter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., Van Montagu M., Rogers J.,
RA Cronin A., Quail M., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA Montfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sehkon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L., Nelson J.,
RA Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffmann J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5] {ECO:0000313|EMBL:CAB52473.1}
RP NUCLEOTIDE SEQUENCE.
RA Legen J., Misera S., Herrmann R.G., Altschmied L.;
RT "Sequences and map position of 31 Arabidopsis thaliana cDNAs encoding
RT organellar polypeptides.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:CAB79944.1}
RP NUCLEOTIDE SEQUENCE.
RA Weichselgartner M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Mewes H.W., Lemcke K., Mayer K.F.X.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:AAL24209.1}
RP NUCLEOTIDE SEQUENCE.
RA Cheuk R., Chen H., Kim C.J., Koesema E., Meyers M.C., Banh J., Bowser L.,
RA Carninci P., Dale J.M., Goldsmith A.D., Hayashizaki Y., Ishida J.,
RA Jiang P.X., Jones T., Kamiya A., Karlin-Neumann G., Kawai J., Lam B.,
RA Lee J.M., Lin J., Liu S.X., Miranda M., Narusaka M., Nguyen M.,
RA Onodera C.S., Palm C.J., Pham P.K., Quach H.L., Sakurai T., Satou M.,
RA Seki M., Southwick A., Tang C.C., Toriumi M., Yamada K., Yamamura Y.,
RA Yu G., Yu S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:AAM63254.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12093376;
RA Haas B.J., Volfovsky N., Town C.D., Troukhan M., Alexandrov N.,
RA Feldmann K.A., Flavell R.B., White O., Salzberg S.L.;
RT "Full-length messenger RNA sequences greatly improve genome annotation.";
RL Genome Biol. 3:RESEARCH0029-RESEARCH0029(2002).
RN [9] {ECO:0000313|EMBL:AAM63254.1}
RP NUCLEOTIDE SEQUENCE.
RA Brover V., Troukhan M., Alexandrov N., Lu Y.-P., Flavell R., Feldmann K.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [10] {ECO:0000313|EMBL:AAM63254.1}
RP NUCLEOTIDE SEQUENCE.
RA Alexandrov N.A., Troukhan M.E., Brover V.V., Flavell R.B., Feldmann K.A.;
RT "Features of Arabidopsis genes and genome discovered using full-length
RT cDNAs.";
RL Plant Mol. Biol. 60:71-87(2006).
RN [11] {ECO:0007829|PubMed:19376835}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12] {ECO:0000313|EMBL:AEE86027.1}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [13] {ECO:0000313|EMBL:AEE86027.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [14] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation.
CC {ECO:0000256|ARBA:ARBA00025198}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family.
CC {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|RuleBase:RU003848}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY058101; AAL24209.1; -; mRNA.
DR EMBL; AY086044; AAM63254.1; -; mRNA.
DR EMBL; CP002687; AEE86027.1; -; Genomic_DNA.
DR EMBL; AL021811; CAA16964.1; -; Genomic_DNA.
DR EMBL; AJ245574; CAB52473.1; -; mRNA.
DR EMBL; AL161580; CAB79944.1; -; Genomic_DNA.
DR PIR; T05402; T05402.
DR RefSeq; NP_194953.1; NM_119378.4.
DR AlphaFoldDB; Q42139; -.
DR SMR; Q42139; -.
DR STRING; 3702.Q42139; -.
DR PaxDb; 3702-AT4G32260-1; -.
DR ProteomicsDB; 179096; -.
DR EnsemblPlants; AT4G32260.1; AT4G32260.1; AT4G32260.
DR GeneID; 829359; -.
DR Gramene; AT4G32260.1; AT4G32260.1; AT4G32260.
DR KEGG; ath:AT4G32260; -.
DR Araport; AT4G32260; -.
DR TAIR; AT4G32260; PDE334.
DR eggNOG; ENOG502S8NX; Eukaryota.
DR HOGENOM; CLU_079215_0_1_1; -.
DR OMA; PLMAIQF; -.
DR OrthoDB; 314390at2759; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42139; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR HAMAP; MF_01399; ATP_synth_bprime; 1.
DR InterPro; IPR034679; ATP_synth_b.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR PANTHER; PTHR33445:SF2; ATP SYNTHASE SUBUNIT B; 1.
DR PANTHER; PTHR33445; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR Pfam; PF00430; ATP-synt_B; 1.
PE 1: Evidence at protein level;
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU003848};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU003848}; Hydrolase {ECO:0000313|EMBL:CAB52473.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU003848}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q42139,
KW ECO:0007829|ProteomicsDB:Q42139};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003848};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003848}.
FT COILED 121..211
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 219 AA; 23918 MW; B60440DD8998C48E CRC64;
MAANSIMASS KPLISLSSNQ QPNRVQIPKF AKLPQIPKSL TSSTDLRSKA LSLSSATAKS
LALIAAFAPP SMAEAMEKAQ LFDFNLTLPI IVVEFLFLMF ALDKVYYSPL GNFMDQRDAS
IKEKLASVKD TSTEVKELDE QAAAVMRAAR AEIAAALNKM KKETQVEVEE KLAEGRKKVE
EELKEALASL ESQKEETIKA LDSQIAALSE DIVKKVLPS
//