ID   AATP6_ARATH             Reviewed;         492 AA.
AC   Q9LH83; F4J0B1;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=AAA-ATPase At3g28520;
DE            EC=3.6.1.- {ECO:0000250|UniProtKB:Q9FLD5};
GN   OrderedLocusNames=At3g28520 {ECO:0000312|EMBL:AEE77455.1};
GN   ORFNames=T20D4.3 {ECO:0000312|EMBL:BAB01954.1};
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;
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   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEE77455.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP002059; BAB01954.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77455.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_189493.1; NM_113772.1.
DR   AlphaFoldDB; Q9LH83; -.
DR   SMR; Q9LH83; -.
DR   STRING; 3702.AT3G28520.1; -.
DR   PaxDb; Q9LH83; -.
DR   PeptideAtlas; Q9LH83; -.
DR   PRIDE; Q9LH83; -.
DR   EnsemblPlants; AT3G28520.1; AT3G28520.1; AT3G28520.
DR   GeneID; 822482; -.
DR   Gramene; AT3G28520.1; AT3G28520.1; AT3G28520.
DR   KEGG; ath:AT3G28520; -.
DR   Araport; AT3G28520; -.
DR   TAIR; locus:2098638; AT3G28520.
DR   eggNOG; KOG0743; Eukaryota.
DR   OrthoDB; 532729at2759; -.
DR   PhylomeDB; Q9LH83; -.
DR   PRO; PR:Q9LH83; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LH83; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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   ATP-binding; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..492
FT                   /note="AAA-ATPase At3g28520"
FT                   /id="PRO_0000434708"
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          313..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         249..256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   492 AA;  57108 MW;  0462D03131D93589 CRC64;
     MLEVGTIWGF TSTTMASIMF LWPMYKQFVP YQLREYLENT IQKYLDKLFR RDSNFVYIRF
     PEYTGEGLSK SRAYDEIGNY LSSISTARAK RLKAKESENS KSLVLCLDDD EAVVVVFQGV
     NVVWSSTVVD KEDKHNSKEG RYLTLTFENH HRDIITNTYI DHVLREGKEI ALKNRERKLY
     TNNDSSSYSS WWEGLWSNVP FNHHASFETL GMDLDKKEEI KKDLIKFTKG KDYYRKVAKP
     WKRGYLLFGP PGTGKSTMIS AIANFLEYDV YDLELTTVKD NAELKKLMLD TKGKSIVVIE
     DIDCSLELTE HRKKKKEEDE DKEEKKEAEN LKRVSGNNES NVTLSGLLNA IDGLWSACSD
     EKIIIFTTNF VDNLDPALIR RGRMDYHIEM SYCRFEAFKV LAKNYLENES HDLYGEIGRL
     LEEVDVSPAD VAENLMPKSD EDDADICFRR LVKSLEEEKK KKIEKEARKN KKKAEDNVKQ
     EKQNKVKGMV TK