CLPP2_ARATH
ID CLPP2_ARATH Reviewed; 241 AA.
AC Q9FN42;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 2, mitochondrial {ECO:0000303|PubMed:11299370};
DE EC=3.4.21.92;
DE AltName: Full=ATP-dependent Clp protease proteolytic subunit 1, mitochondrial;
DE AltName: Full=Endopeptidase ClpP2 {ECO:0000303|PubMed:11299370};
DE AltName: Full=nClpP7;
DE Flags: Precursor;
GN Name=CLPP2 {ECO:0000303|PubMed:11299370}; Synonyms=NCLPP7;
GN OrderedLocusNames=At5g23140 {ECO:0000312|Araport:AT5G23140};
GN ORFNames=MYJ24.13 {ECO:0000312|EMBL:BAB09831.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 PROTEIN SEQUENCE OF 143-163; 175-185 AND 211-228, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=11278690; DOI=10.1074/jbc.m010503200;
RA Peltier J.-B., Ytterberg J., Liberles D.A., Roepstorff P., van Wijk K.J.;
RT "Identification of a 350-kDa ClpP protease complex with 10 different Clp
RT isoforms in chloroplasts of Arabidopsis thaliana.";
RL J. Biol. Chem. 276:16318-16327(2001).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, 3D-STRUCTURE
RP MODELING, AND SUBUNIT.
RX PubMed=14593120; DOI=10.1074/jbc.m309212200;
RA Peltier J.-B., Ripoll D.R., Friso G., Rudella A., Cai Y., Ytterberg J.,
RA Giacomelli L., Pillardy J., van Wijk K.J.;
RT "Clp protease complexes from photosynthetic and non-photosynthetic plastids
RT and mitochondria of plants, their predicted three-dimensional structures,
RT and functional implications.";
RL J. Biol. Chem. 279:4768-4781(2004).
RN [9]
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).
RN [10]
RP REVIEW.
RX PubMed=22085372; DOI=10.1111/j.1399-3054.2011.01541.x;
RA Clarke A.K.;
RT "The chloroplast ATP-dependent Clp protease in vascular plants - new
RT dimensions and future challenges.";
RL Physiol. Plantarum 145:235-244(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP TYR-30.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Component of the mitochondrial ATP-dependent Clp protease
CC (PubMed:11352464). Cleaves peptides in various proteins in a process
CC that requires ATP hydrolysis (By similarity). Has a chymotrypsin-like
CC activity. Plays a major role in the degradation of misfolded proteins
CC (By similarity). {ECO:0000250|UniProtKB:Q27539,
CC ECO:0000269|PubMed:11352464}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins to small peptides in the presence of
CC ATP and magnesium. alpha-casein is the usual test substrate. In the
CC absence of ATP, only oligopeptides shorter than five residues are
CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC occurs).; EC=3.4.21.92;
CC -!- SUBUNIT: Homotetradecamer. {ECO:0000269|PubMed:14593120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11352464,
CC ECO:0000269|PubMed:14593120, ECO:0000305|PubMed:25732537}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in leaves, shoots, roots
CC and flowers. {ECO:0000269|PubMed:11352464}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR EMBL; AB006708; BAB09831.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93126.1; -; Genomic_DNA.
DR EMBL; AK118523; BAC43126.1; -; mRNA.
DR EMBL; BT005261; AAO63325.1; -; mRNA.
DR RefSeq; NP_568427.1; NM_122220.5.
DR AlphaFoldDB; Q9FN42; -.
DR SMR; Q9FN42; -.
DR STRING; 3702.AT5G23140.1; -.
DR MEROPS; S14.A02; -.
DR PaxDb; Q9FN42; -.
DR PRIDE; Q9FN42; -.
DR ProteomicsDB; 246659; -.
DR EnsemblPlants; AT5G23140.1; AT5G23140.1; AT5G23140.
DR GeneID; 832378; -.
DR Gramene; AT5G23140.1; AT5G23140.1; AT5G23140.
DR KEGG; ath:AT5G23140; -.
DR Araport; AT5G23140; -.
DR TAIR; locus:2178282; AT5G23140.
DR eggNOG; KOG0840; Eukaryota.
DR HOGENOM; CLU_058707_3_1_1; -.
DR InParanoid; Q9FN42; -.
DR OMA; GFKRQDP; -.
DR OrthoDB; 1274502at2759; -.
DR PhylomeDB; Q9FN42; -.
DR PRO; PR:Q9FN42; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN42; baseline and differential.
DR Genevisible; Q9FN42; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0009840; C:chloroplastic endopeptidase Clp complex; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009532; C:plastid stroma; IDA:TAIR.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR CDD; cd07017; S14_ClpP_2; 1.
DR HAMAP; MF_00444; ClpP; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR InterPro; IPR033135; ClpP_His_AS.
DR InterPro; IPR018215; ClpP_Ser_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Mitochondrion; Protease;
KW Reference proteome; Serine protease; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 31..241
FT /note="ATP-dependent Clp protease proteolytic subunit 2,
FT mitochondrial"
FT /id="PRO_0000308977"
FT ACT_SITE 127
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q27539"
FT ACT_SITE 152
FT /evidence="ECO:0000250|UniProtKB:Q27539"
SQ SEQUENCE 241 AA; 26283 MW; DFC93372387E542A CRC64;
MMRGLVSGAK MLSSTPSSMA TSIATGRRSY SLIPMVIEHS SRGERAYDIF SRLLKERIIC
INGPINDDTS HVVVAQLLYL ESENPSKPIH MYLNSPGGHV TAGLAIYDTM QYIRSPISTI
CLGQAASMAS LLLAAGAKGQ RRSLPNATVM IHQPSGGYSG QAKDITIHTK QIVRVWDALN
ELYVKHTGQP LDVVANNMDR DHFMTPEEAK AFGIIDEVID ERPLELVKDA VGNESKDKSS
S
