CLPP1_ARATH
ID CLPP1_ARATH Reviewed; 196 AA.
AC P56772; Q3ZVD5; Q9XQZ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Chloroplastic ATP-dependent Clp protease proteolytic subunit 1 {ECO:0000303|PubMed:11299370};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase ClpP1 {ECO:0000303|PubMed:11299370};
DE Short=pClpP;
GN Name=clpP1 {ECO:0000303|PubMed:11299370}; Synonyms=ClpP;
GN OrderedLocusNames=AtCg00670 {ECO:0000312|Araport:ATCG00670};
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
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=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10427773; DOI=10.1093/oxfordjournals.pcp.a029571;
RA Nakabayashi K., Ito M., Kiyosue T., Shinozaki K., Watanabe A.;
RT "Identification of clp genes expressed in senescing Arabidopsis leaves.";
RL Plant Cell Physiol. 40:504-514(1999).
RN [3]
RP PROTEIN SEQUENCE OF 12-26 AND 123-149, SUBUNIT, AND IDENTIFICATION BY MASS
RP 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 [4]
RP SUBCELLULAR LOCATION.
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-195, AND RNA EDITING.
RC STRAIN=cv. Cvi-0, and cv. Wassilewskija;
RX PubMed=16115067; DOI=10.1111/j.1365-313x.2005.02484.x;
RA Tillich M., Funk H.T., Schmitz-Linneweber C., Poltnigg P., Sabater B.,
RA Martin M., Maier R.M.;
RT "Editing of plastid RNA in Arabidopsis thaliana ecotypes.";
RL Plant J. 43:708-715(2005).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=11982939; DOI=10.1034/j.1399-3054.2002.1140113.x;
RA Zheng B., Halperin T., Hruskova-Heidingsfeldova O., Adam Z., Clarke A.K.;
RT "Characterization of chloroplast Clp proteins in Arabidopsis: localization,
RT tissue specificity and stress responses.";
RL Physiol. Plantarum 114:92-101(2002).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16766689; DOI=10.1105/tpc.106.042861;
RA Rudella A., Friso G., Alonso J.M., Ecker J.R., van Wijk K.J.;
RT "Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS
RT protease complex and defects in chloroplast biogenesis in Arabidopsis.";
RL Plant Cell 18:1704-1721(2006).
RN [10]
RP SUBUNIT.
RX PubMed=16980539; DOI=10.1105/tpc.106.044594;
RA Sjoegren L.L.E., Stanne T.M., Zheng B., Sutinen S., Clarke A.K.;
RT "Structural and functional insights into the chloroplast ATP-dependent Clp
RT protease in Arabidopsis.";
RL Plant Cell 18:2635-2649(2006).
RN [11]
RP 3D-STRUCTURE MODELING, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=21712416; DOI=10.1105/tpc.111.086454;
RA Olinares P.D., Kim J., Davis J.I., van Wijk K.J.;
RT "Subunit stoichiometry, evolution, and functional implications of an
RT asymmetric plant plastid ClpP/R protease complex in Arabidopsis.";
RL Plant Cell 23:2348-2361(2011).
RN [13]
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).
CC -!- FUNCTION: Cleaves peptides in various proteins in a process that
CC requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a
CC major role in the degradation of misfolded proteins.
CC {ECO:0000255|HAMAP-Rule:MF_00444}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00444};
CC -!- SUBUNIT: Component of the chloroplastic Clp protease core complex which
CC consist of at least 16 proteins: CLPP4 (3 copies), CLPP5 (3 copies),
CC CLPR4 (2 copies), ClpP1 (1 copy), CLPP6 (1 copy), CLPR2 (1 copy), CLPT1
CC (1 copy), CLPT2 (1 copy) and 3 copies of CLPP3 and/or CLPR1 and/or
CC CLPR3 (PubMed:11278690, PubMed:14593120, PubMed:16766689,
CC PubMed:16980539). The core complex is organized in two heptameric
CC rings, one containing CLPP3,4,5,6 in a 1:2:3:1 ratio and the other
CC CLPP1 and CLPR1,2,3,4 in a 3:1:1:1:1 ratio (PubMed:21712416).
CC {ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:11278690,
CC ECO:0000269|PubMed:14593120, ECO:0000269|PubMed:16766689,
CC ECO:0000269|PubMed:16980539, ECO:0000269|PubMed:21712416}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:10427773, ECO:0000269|PubMed:11352464,
CC ECO:0000269|PubMed:11982939, ECO:0000269|PubMed:14593120}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves. Also detected in stems,
CC and to a lower extent, in roots (at protein level).
CC {ECO:0000269|PubMed:11982939}.
CC -!- INDUCTION: Repressed in darkness. Slightly induced by high light stress
CC and during cold acclimation (at protein level).
CC {ECO:0000269|PubMed:10427773, ECO:0000269|PubMed:11982939}.
CC -!- RNA EDITING: Modified_positions=187 {ECO:0000269|PubMed:16115067};
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
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DR EMBL; AP000423; BAA84410.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB022325; BAA82063.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ971664; CAI99002.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ971665; CAI99003.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_051083.1; NC_000932.1.
DR AlphaFoldDB; P56772; -.
DR SMR; P56772; -.
DR BioGRID; 29940; 7.
DR IntAct; P56772; 10.
DR STRING; 3702.ATCG00670.1; -.
DR MEROPS; S14.002; -.
DR PaxDb; P56772; -.
DR PeptideAtlas; P56772; -.
DR PRIDE; P56772; -.
DR ProteomicsDB; 246657; -.
DR GeneID; 844734; -.
DR KEGG; ath:ArthCp048; -.
DR Araport; ATCG00670; -.
DR eggNOG; KOG0840; Eukaryota.
DR HOGENOM; CLU_058707_4_2_1; -.
DR InParanoid; P56772; -.
DR OrthoDB; 1274502at2759; -.
DR BRENDA; 3.4.21.92; 399.
DR PRO; PR:P56772; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P56772; baseline and differential.
DR Genevisible; P56772; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
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:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
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 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.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Hydrolase; Plastid; Protease;
KW Reference proteome; RNA editing; Serine protease.
FT CHAIN 1..196
FT /note="Chloroplastic ATP-dependent Clp protease proteolytic
FT subunit 1"
FT /id="PRO_0000179734"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 126
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ SEQUENCE 196 AA; 22124 MW; 2BB430CFB5B5F609 CRC64;
MPIGVPKVPF RSPGEGDTSW VDIYNRLYRE RLFFLGQEVD TEISNQLISL MIYLSIEKDT
KDLYLFINSP GGWVISGMAI YDTMQFVRPD VQTICMGLAA SIASFILVGG AITKRIAFPH
ARVMIHQPAS SFYEAQTGEF ILEAEELLKL RETITRVYVQ RTGKPIWVIS EDMERDVFMS
ATEAQAYGIV DLVAVQ
