ID   AATP7_ARATH             Reviewed;         510 AA.
AC   Q9LH82; Q2V3R7;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=AAA-ATPase At3g28540;
DE            EC=3.6.1.- {ECO:0000250|UniProtKB:Q9FLD5};
GN   OrderedLocusNames=At3g28540 {ECO:0000312|EMBL:AEE77457.1};
GN   ORFNames=T20D4.4 {ECO:0000312|EMBL:BAB01955.1};
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:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LH82-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LH82-2; Sequence=VSP_057974;
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP002059; BAB01955.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77457.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77458.1; -; Genomic_DNA.
DR   RefSeq; NP_001030789.1; NM_001035712.1. [Q9LH82-2]
DR   RefSeq; NP_189495.1; NM_113774.3. [Q9LH82-1]
DR   AlphaFoldDB; Q9LH82; -.
DR   STRING; 3702.AT3G28540.1; -.
DR   iPTMnet; Q9LH82; -.
DR   PaxDb; Q9LH82; -.
DR   PRIDE; Q9LH82; -.
DR   ProteomicsDB; 244622; -. [Q9LH82-1]
DR   EnsemblPlants; AT3G28540.1; AT3G28540.1; AT3G28540. [Q9LH82-1]
DR   EnsemblPlants; AT3G28540.2; AT3G28540.2; AT3G28540. [Q9LH82-2]
DR   GeneID; 822484; -.
DR   Gramene; AT3G28540.1; AT3G28540.1; AT3G28540. [Q9LH82-1]
DR   Gramene; AT3G28540.2; AT3G28540.2; AT3G28540. [Q9LH82-2]
DR   KEGG; ath:AT3G28540; -.
DR   Araport; AT3G28540; -.
DR   TAIR; locus:2098648; AT3G28540.
DR   eggNOG; KOG0743; Eukaryota.
DR   InParanoid; Q9LH82; -.
DR   OMA; ANVISWA; -.
DR   OrthoDB; 532729at2759; -.
DR   PhylomeDB; Q9LH82; -.
DR   PRO; PR:Q9LH82; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LH82; baseline and differential.
DR   Genevisible; Q9LH82; AT.
DR   GO; GO:0016021; C:integral component of membrane; 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:0006950; P:response to stress; IEA:UniProt.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR025753; AAA_N_dom.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF14363; AAA_assoc; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; ATP-binding; Hydrolase; Magnesium; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..510
FT                   /note="AAA-ATPase At3g28540"
FT                   /id="PRO_0000434709"
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          460..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         246..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         508..510
FT                   /note="NHI -> K (in isoform 2)"
FT                   /id="VSP_057974"
SQ   SEQUENCE   510 AA;  59151 MW;  D372C2CD616DC111 CRC64;
     MFEAGGLFGF TGTTMASLMF FWSVYRQFVP YQIRDYLEKC FYKMFGLVSN SVHIKFTEYT
     EDKGLKKSQA YDLIRNYLSS KSTARAQRLK ANESKNSKSL VLSLDNHEAV EDVFQGVKVV
     WSLSVWKSND QADSSEKRYL TLSFHNRYRE MITTTYLDHV LREGKEIGLK NRERKLYTNN
     SSQDYSAWRE GRWSNVPFDH PATFETLAMD LEKKEGMKKD LIKFTKGKDY YRKVGKPWKR
     GYLLFGPPGT GKSTMISAMA NFLEYDVYDL ELTTVKDNSE LKKLMLDTKG KSIVVIEDID
     CSLDLTGQRK KKKEEDEDEE EEEKKKEAEK LLKRERGERE SKVTLSGLLN AIDGLWSACS
     GEKIIVFTTN YLDKLDPALI RRGRMDNHIE MSYCRFEAFK VLAKNYLEIE SHDLFGEIKR
     LVEETDMSPA DVAENLMPKS DEDDADICLT RLVKSLEEEK EKAKKLAEEE KMKKAARDAR
     RIKKKAEEEH KKKNKVEENG DVSHDNGNHI