CLPX3_ARATH
ID CLPX3_ARATH Reviewed; 656 AA.
AC Q66GN9; Q9C814; Q9C874;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=CLP protease regulatory subunit CLPX3, mitochondrial {ECO:0000303|Ref.4};
DE Flags: Precursor;
GN Name=CLPX3 {ECO:0000303|Ref.4};
GN OrderedLocusNames=At1g33360 {ECO:0000312|Araport:AT1G33360};
GN ORFNames=F10C21.5 {ECO:0000312|EMBL:AAG51217.1},
GN T16O9.5 {ECO:0000312|EMBL:AAG51286.1};
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|EMBL:AAU05486.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NOMENCLATURE.
RX DOI=10.1111/j.1399-3054.2005.00452.x;
RA Clarke A.K., MacDonald T.M., Sjoegren L.L.;
RT "The ATP-dependent Clp protease in chloroplasts of higher plants.";
RL Physiol. Plantarum 123:406-412(2005).
CC -!- FUNCTION: ATP-dependent specificity component of the mitochondrial Clp
CC protease. It directs the protease to specific substrates. Can perform
CC chaperone functions in the absence of ClpP.
CC {ECO:0000250|UniProtKB:B1J693}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51217.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51286.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AC027035; AAG51286.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC051630; AAG51217.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31587.1; -; Genomic_DNA.
DR EMBL; BT015363; AAU05486.1; -; mRNA.
DR EMBL; BT015893; AAU95429.1; -; mRNA.
DR PIR; D86457; D86457.
DR RefSeq; NP_564423.3; NM_103063.4.
DR AlphaFoldDB; Q66GN9; -.
DR SMR; Q66GN9; -.
DR STRING; 3702.AT1G33360.1; -.
DR iPTMnet; Q66GN9; -.
DR PaxDb; Q66GN9; -.
DR PRIDE; Q66GN9; -.
DR ProteomicsDB; 222098; -.
DR EnsemblPlants; AT1G33360.1; AT1G33360.1; AT1G33360.
DR GeneID; 840230; -.
DR Gramene; AT1G33360.1; AT1G33360.1; AT1G33360.
DR KEGG; ath:AT1G33360; -.
DR Araport; AT1G33360; -.
DR TAIR; locus:2006942; AT1G33360.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_6_0_1; -.
DR InParanoid; Q66GN9; -.
DR OMA; PRGHQRI; -.
DR OrthoDB; 1040247at2759; -.
DR PhylomeDB; Q66GN9; -.
DR PRO; PR:Q66GN9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q66GN9; baseline and differential.
DR Genevisible; Q66GN9; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Mitochondrion; Nucleotide-binding; Protease;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..656
FT /note="CLP protease regulatory subunit CLPX3,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434550"
FT REGION 142..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 316..323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:B1J693"
SQ SEQUENCE 656 AA; 71540 MW; 817AB68E5BCC34A3 CRC64;
MSGLWRLRNL KSLALHARSI SPVSNLYSLE LGSCPRRRIQ ERFKSEQGGG GGGGDDFPVP
VTRRKLRAEP NCPRCSKQMD LLFSNRQFPS SNLLQRPDDS DSSGAGDKTN FQSVNFCPTC
KTAYGFNPRG VSPLQGTFIE IGRVQSPTTT TTNATTSKST RKQQQHSKDP NQGFNYRNKL
RSSFWDTLRS YGAEPPEDWS PPPPHSPLNS SPPNTIPVNA SPSAVDTSPL PDAVNDVSRW
GGAGLGRDFP TPKEICKWLD KFVIGQSRAK KVLSVAVYNH YKRIYHTSMK KGSAAQPIDD
DDNVELDKSN VLLMGPTGSG KTLLAKTLAR LVNVPFVIAD ATTLTQAGYV GDDVESILHK
LLTVAEFNVQ AAQQGIVYID EVDKITKKAE SLNISRDVSG EGVQQALLKL LEGTIVNVPG
KGARKHPRGD HIQIDTKDIL FICGGAFVDL EKTIVDRRQD SSIGFGAPVR ANMATSGVTS
GAITSSLLES VESADLTAYG LIPEFVGRFP ILVSLSALTE DQLIRVLVEP KNALGKQYKK
LFSMNNVKLH FTEKALEIIS KQAMVKNTGA RGLRALLESI LTEAMFEIPD DKKGDERIDA
VIVDEESTSS EASRGCTAKI LRGDGAFERY LSENKSKDAT EPMVDERVGS AKAMRL
