AATP2_ARATH
ID AATP2_ARATH Reviewed; 494 AA.
AC F4IQG2; Q9SI12;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=AAA-ATPase At2g18190;
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q9FLD5};
GN OrderedLocusNames=At2g18190 {ECO:0000312|EMBL:AEC06736.1};
GN ORFNames=F8D23 {ECO:0000305};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
RN [3]
RP INDUCTION BY SALT.
RC STRAIN=cv. Columbia;
RX PubMed=16510518; DOI=10.1093/jxb/erj098;
RA Ma S., Gong Q., Bohnert H.J.;
RT "Dissecting salt stress pathways.";
RL J. Exp. Bot. 57:1097-1107(2006).
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 -!- INDUCTION: Induced in roots by salt stress.
CC {ECO:0000269|PubMed:16510518}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31347.1; Type=Erroneous gene model prediction; Note=The predicted gene At2g18190 has been split into 2 genes: At2g18190 and At2g18193.; Evidence={ECO:0000305};
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DR EMBL; AC007212; AAD31347.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06736.1; -; Genomic_DNA.
DR PIR; D84561; D84561.
DR RefSeq; NP_179411.2; NM_127376.3.
DR AlphaFoldDB; F4IQG2; -.
DR SMR; F4IQG2; -.
DR STRING; 3702.AT2G18190.1; -.
DR PaxDb; F4IQG2; -.
DR PRIDE; F4IQG2; -.
DR ProteomicsDB; 244344; -.
DR EnsemblPlants; AT2G18190.1; AT2G18190.1; AT2G18190.
DR GeneID; 816332; -.
DR Gramene; AT2G18190.1; AT2G18190.1; AT2G18190.
DR KEGG; ath:AT2G18190; -.
DR Araport; AT2G18190; -.
DR TAIR; locus:2053109; AT2G18190.
DR eggNOG; KOG0743; Eukaryota.
DR HOGENOM; CLU_010189_0_1_1; -.
DR OMA; KQKHLNV; -.
DR OrthoDB; 532729at2759; -.
DR PRO; PR:F4IQG2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IQG2; baseline and differential.
DR Genevisible; F4IQG2; 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:0009651; P:response to salt stress; IEP:UniProtKB.
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; IPR003960; ATPase_AAA_CS.
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.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..494
FT /note="AAA-ATPase At2g18190"
FT /id="PRO_0000434704"
FT TRANSMEM 13..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 459..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..494
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 494 AA; 56289 MW; 7D0DB0368A9699EF CRC64;
MFPSISNISL SPSSLFTAYA SLTGFLMLFR SLFNDEVPER LRSYITDLLN RFFTPKSKNL
TMVIDEIIGF KRNQVFDAAE VYLRNKIGPE TARLRVGKLP KQKHFTIYIE KGEEILDTFE
NSELRWTYVE SENEASQKEK RYYELTFEKK LRDKVMNSYL SHVVAESEET KRDLRAVKLY
SRDVRASKDD DGMAGAGWGC INLEHPSTFE TLAMDPGAKK KIIDDMERFL KRREFYKRVG
KAWKRGYLLY GPPGTGKSSL IAAMANYLKF DVFDLELSSI YENAQLKSIL LSTTNRSILV
IEDIDCSSAE VVDREADEYQ EYEEGYYGRV TLSGLLNFVD GLWSSFGDER IIVFTTNHKE
RLDPALLRPG RMDMHINMSY CTGLGFRTLV SNYLGLGGLN HPLCEEIEAL IDSTEVTPAE
LAEELMQEDD TDVVLRGVVS FVENRKVEIS KTKELEGSTC RKLDGDDKHN VSSTNDLKKT
KKKKKGGKGK AKGN
