CLPX1_ARATH
ID CLPX1_ARATH Reviewed; 579 AA.
AC Q9FK07; O48566;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=CLP protease regulatory subunit CLPX1, mitochondrial {ECO:0000303|PubMed:11299370};
DE Flags: Precursor;
GN Name=CLPX1 {ECO:0000303|PubMed:11299370};
GN OrderedLocusNames=At5g53350 {ECO:0000312|Araport:AT5G53350};
GN ORFNames=K19E1.15 {ECO:0000312|EMBL:BAB09797.1};
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RX PubMed=11352464; DOI=10.1023/a:1010677220323;
RA Halperin T., Zheng B., Itzhaki H., Clarke A.K., Adam Z.;
RT "Plant mitochondria contain proteolytic and regulatory subunits of the ATP-
RT dependent Clp protease.";
RL Plant Mol. Biol. 45:461-468(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
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 [4]
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 [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11299370; DOI=10.1104/pp.125.4.1912;
RA Adam Z., Adamska I., Nakabayashi K., Ostersetzer O., Haussuhl K.,
RA Manuell A., Zheng B., Vallon O., Rodermel S.R., Shinozaki K., Clarke A.K.;
RT "Chloroplast and mitochondrial proteases in Arabidopsis. A proposed
RT nomenclature.";
RL Plant Physiol. 125:1912-1918(2001).
RN [6]
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 (PubMed:11352464). It directs the protease to specific
CC substrates (By similarity). Can perform chaperone functions in the
CC absence of ClpP (By similarity). {ECO:0000250|UniProtKB:B1J693,
CC ECO:0000269|PubMed:11352464}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11352464}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in leaves, shoots, roots
CC and flowers. {ECO:0000269|PubMed:11352464}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000305}.
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DR EMBL; AF036328; AAB88706.1; -; mRNA.
DR EMBL; AB013388; BAB09797.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96343.1; -; Genomic_DNA.
DR EMBL; AY035103; AAK59608.1; -; mRNA.
DR EMBL; AY142561; AAN13130.1; -; mRNA.
DR RefSeq; NP_568792.1; NM_124714.4.
DR AlphaFoldDB; Q9FK07; -.
DR SMR; Q9FK07; -.
DR STRING; 3702.AT5G53350.1; -.
DR PaxDb; Q9FK07; -.
DR PRIDE; Q9FK07; -.
DR ProteomicsDB; 222097; -.
DR EnsemblPlants; AT5G53350.1; AT5G53350.1; AT5G53350.
DR GeneID; 835416; -.
DR Gramene; AT5G53350.1; AT5G53350.1; AT5G53350.
DR KEGG; ath:AT5G53350; -.
DR Araport; AT5G53350; -.
DR TAIR; locus:2154257; AT5G53350.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_6_1_1; -.
DR InParanoid; Q9FK07; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 1040247at2759; -.
DR PhylomeDB; Q9FK07; -.
DR PRO; PR:Q9FK07; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK07; baseline and differential.
DR Genevisible; Q9FK07; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..579
FT /note="CLP protease regulatory subunit CLPX1,
FT mitochondrial"
FT /id="PRO_0000434548"
FT REGION 99..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:B1J693"
FT CONFLICT 132
FT /note="S -> N (in Ref. 1; AAB88706)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="N -> Y (in Ref. 1; AAB88706)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="N -> T (in Ref. 1; AAB88706)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="S -> T (in Ref. 1; AAB88706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 61964 MW; AF8CF9E9217AE7FB CRC64;
MAAALRSNTS RETASLTLSH FRYFIFNRIH TARTATSPPH CNHRSKSDEK FPYKISSLGT
SFLDNRGGGE RRNSTKCYAA QKKLSGVGSS VVILSSQGDP PDLWQPPGDG VSVRVNGSSV
NLGRGGGGGG SSPGGPGNGT GSNSKEDCWG GSNLGSDFPT PKEICKGLNK FVIGQERAKK
VLSVAVYNHY KRIYHESSQK RSAGETDSTA AKPADDDMVE LEKSNILLMG PTGSGKTLLA
KTLARFVNVP FVIADATTLT QAGYVGEDVE SILYKLLTVA DYNVAAAQQG IVYIDEVDKI
TKKAESLNIS RDVSGEGVQQ ALLKMLEGTI VNVPEKGARK HPRGDNIQID TKDILFICGG
AFVDIEKTIS ERRHDSSIGF GAPVRANMRA GGVTNAAVAS NLMETVESSD LIAYGLIPEF
VGRFPVLVSL SALTENQLMQ VLTEPKNALG KQYKKMYQMN SVKLHFTESA LRLIARKAIT
KNTGARGLRA LLESILMDSM YEIPDEGTGS DMIEAVVVDE EAVEGEGRRG SGAKILRGKG
ALARYLSETN SKDSPQTTKE GSDGETEVEA EIPSVVASM
