CLPX2_ARATH
ID CLPX2_ARATH Reviewed; 608 AA.
AC F4K7F6; Q9LTA9;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=CLP protease regulatory subunit CLPX2, mitochondrial {ECO:0000303|PubMed:11299370};
DE Flags: Precursor;
GN Name=CLPX2 {ECO:0000303|PubMed:11299370};
GN OrderedLocusNames=At5g49840 {ECO:0000312|Araport:AT5G49840};
GN ORFNames=K21G20.5 {ECO:0000312|EMBL:BAA98151.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000312|Proteomes:UP000006548};
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 IDENTIFICATION.
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 [4]
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 [5]
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 ---------------------------------------------------------------------------
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; AB025612; BAA98151.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95863.1; -; Genomic_DNA.
DR RefSeq; NP_001332696.1; NM_001344859.1.
DR RefSeq; NP_568714.4; NM_124362.4.
DR AlphaFoldDB; F4K7F6; -.
DR SMR; F4K7F6; -.
DR STRING; 3702.AT5G49840.1; -.
DR iPTMnet; F4K7F6; -.
DR PaxDb; F4K7F6; -.
DR PRIDE; F4K7F6; -.
DR ProteomicsDB; 220530; -.
DR EnsemblPlants; AT5G49840.1; AT5G49840.1; AT5G49840.
DR GeneID; 835047; -.
DR Gramene; AT5G49840.1; AT5G49840.1; AT5G49840.
DR KEGG; ath:AT5G49840; -.
DR Araport; AT5G49840; -.
DR TAIR; locus:2155446; AT5G49840.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_6_0_1; -.
DR InParanoid; F4K7F6; -.
DR OrthoDB; 1040247at2759; -.
DR PRO; PR:F4K7F6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K7F6; baseline and differential.
DR Genevisible; F4K7F6; 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 3: Inferred from homology;
KW ATP-binding; Hydrolase; Mitochondrion; Nucleotide-binding; Protease;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..66
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 67..608
FT /note="CLP protease regulatory subunit CLPX2,
FT mitochondrial"
FT /id="PRO_0000434549"
FT REGION 143..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 270..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:B1J693"
FT CONFLICT 302
FT /note="S -> G (in Ref. 1; BAA98151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 66390 MW; 5F947C35A2928B7A CRC64;
MFCSLSISRF VSRKTITSSS LLSRSFRFLL SVDSPPHIPL LRPSSNTLIP SSSFSRRIWD
SCSGGGGGGG GDDYDHIRSD VNCPRCSAQM HVIFSNRPLS LTAREPGIYQ AVNFCSQCKT
AFYFRPFKLS PLQGSFIELG KVKGTDDDHD DDDDDQKSFP RNWKIQGLRS DEDGEDADEE
EDESNGGDKE KQSVIKLPTP KEICQGLDEF VIGQEKAKKV LSVAVYNHYK RIYHASRKKG
SASESYNIDM EDDNIDHVEL DKSNVLLLGP TGSGKTLLAK TLARIVNVPF AIADATSLTQ
ASYVGEDVES ILYKLYVEAG CNVEEAQRGI VYIDEVDKMT MKSHSSNGGR DVSGEGVQQS
LLKLLEGTVV SVPIPEKGLR RDPRGDSIQM DTKDILFICG GAFIDLEKTV SERQHDASIG
FGASVRTNMS TSGLSSAAVT SSLLESLQSE DLVAYGLIPE FVGRLPILVS LSALNEDQLV
QVLTEPKSAL GKQYKKLFRM NNVQLQFTEG ATRLIARKAM SKNTGARGLR SILESILTEA
MFEVPDSITE GSQSIKAVLV DEEAVGSVGS PGCGAKILKG DNVLQQFVEE AESKEKSKED
EAKRAQSM
