GenomeNet

Database: UniProt
Entry: CLPX3_ARATH
LinkDB: CLPX3_ARATH
Original site: 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   24-JAN-2024, entry version 153.
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.Q66GN9; -.
DR   iPTMnet; Q66GN9; -.
DR   PaxDb; 3702-AT1G33360-1; -.
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; AT1G33360; -.
DR   eggNOG; KOG0745; Eukaryota.
DR   HOGENOM; CLU_014218_6_0_1; -.
DR   InParanoid; Q66GN9; -.
DR   OMA; ANMRNGA; -.
DR   OrthoDB; 452393at2759; -.
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:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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
//
DBGET integrated database retrieval system