CLPT1_ARATH
ID CLPT1_ARATH Reviewed; 238 AA.
AC Q93WL3; Q9STK0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit CLPT1, chloroplastic {ECO:0000303|Ref.7};
DE AltName: Full=nClpC-like protein {ECO:0000303|PubMed:11278690};
DE Flags: Precursor;
GN Name=CLPT1 {ECO:0000303|Ref.7};
GN Synonyms=CLPS1 {ECO:0000303|PubMed:14593120};
GN OrderedLocusNames=At4g25370 {ECO:0000312|Araport:AT4G25370};
GN ORFNames=T30C3.40 {ECO:0000312|EMBL:CAB45514.1};
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:AAL15176.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
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 IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP 3D-STRUCTURE MODELING.
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 [7]
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 [8]
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=21266658; DOI=10.1105/tpc.110.082321;
RA Sjoegren L.L., Clarke A.K.;
RT "Assembly of the chloroplast ATP-dependent Clp protease in Arabidopsis is
RT regulated by the ClpT accessory proteins.";
RL Plant Cell 23:322-332(2011).
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 INTERACTION WITH CLPS1.
RX PubMed=23898032; DOI=10.1105/tpc.113.112557;
RA Nishimura K., Asakura Y., Friso G., Kim J., Oh S.H., Rutschow H.,
RA Ponnala L., van Wijk K.J.;
RT "ClpS1 is a conserved substrate selector for the chloroplast Clp protease
RT system in Arabidopsis.";
RL Plant Cell 25:2276-2301(2013).
RN [12]
RP SUBUNIT, AND INTERACTION WITH CLPC2 AND CLPD.
RX PubMed=25149061; DOI=10.1186/s12870-014-0228-0;
RA Colombo C.V., Ceccarelli E.A., Rosano G.L.;
RT "Characterization of the accessory protein ClpT1 from Arabidopsis thaliana:
RT oligomerization status and interaction with Hsp100 chaperones.";
RL BMC Plant Biol. 14:228-228(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 64-238, DISRUPTION PHENOTYPE,
RP IDENTIFICATION BY MASS SPECTROMETRY, CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP ALA-64, FUNCTION, INTERACTION WITH CPN21, MUTAGENESIS OF THR-111;
RP 153-MET--PHE-156 AND THR-164, AND DOMAIN.
RX PubMed=25921872; DOI=10.1105/tpc.15.00106;
RA Kim J., Kimber M.S., Nishimura K., Friso G., Schultz L., Ponnala L.,
RA van Wijk K.J.;
RT "Structures, functions, and interactions of ClpT1 and ClpT2 in the Clp
RT protease system of Arabidopsis chloroplasts.";
RL Plant Cell 27:1477-1496(2015).
CC -!- FUNCTION: Accessory protein regulating the assembly of the plastidial
CC Clp protease system (PubMed:21266658, PubMed:25921872). CLPT1 first
CC binds to the heptameric P-ring containing the CLP3-6 subunits followed
CC by CLPT2, and only then does the P-ring combine with the R-ring
CC composed of the clpP1 and CLPR1-4 subunits (PubMed:21266658). Once the
CC core complex is fully assembled, it then associates to the CLPC
CC chaperone partner to form the functional protease (PubMed:21266658).
CC CLPT1 and CLPT2 are partially redundant (PubMed:25921872).
CC {ECO:0000269|PubMed:21266658, ECO:0000269|PubMed:25921872}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:21266658, PubMed:25149061).
CC Binds to the CLP3-6 ring (P-ring) (PubMed:16980539). The dimers
CC monomerize before association to the P-ring (PubMed:21266658).
CC Component of the chloroplastic Clp protease core complex which consist
CC of at least 16 proteins: CLPP4 (3 copies), CLPP5 (3 copies), CLPR4 (2
CC copies), ClpP1 (1 copy), CLPP6 (1 copy), CLPR2 (1 copy), CLPT1 (1
CC copy), CLPT2 (1 copy) and 3 copies of CLPP3 and/or CLPR1 and/or CLPR3
CC (PubMed:11278690, PubMed:14593120). Interacts with CLPC2 and CLPD
CC (PubMed:25149061). Interacts with CPN21 (PubMed:25921872). No
CC interactions with CLPS1 (PubMed:23898032).
CC {ECO:0000269|PubMed:11278690, ECO:0000269|PubMed:14593120,
CC ECO:0000269|PubMed:16980539, ECO:0000269|PubMed:21266658,
CC ECO:0000269|PubMed:23898032, ECO:0000269|PubMed:25149061,
CC ECO:0000269|PubMed:25921872}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11278690, ECO:0000269|PubMed:14593120}.
CC -!- DOMAIN: The MYFF motif is functionally important for stabilization of
CC the overall ClpPR complex. {ECO:0000269|PubMed:25921872}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:21266658,
CC PubMed:25921872). Clpt1 and clpt2 double mutants show delayed
CC development, reduced plant growth, and virescent, serrated leaves
CC (PubMed:25921872). Clpt1 and clpt2 double mutants are seedling lethal
CC under autotrophic conditions (PubMed:21266658).
CC {ECO:0000269|PubMed:21266658, ECO:0000269|PubMed:25921872}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45514.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81348.1; 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; AL079350; CAB45514.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81348.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85048.1; -; Genomic_DNA.
DR EMBL; AY035135; AAK59640.1; -; mRNA.
DR EMBL; AY059070; AAL15176.1; -; mRNA.
DR EMBL; AY086824; AAM63872.1; -; mRNA.
DR PIR; T10217; T10217.
DR RefSeq; NP_567718.1; NM_118669.3.
DR PDB; 4Y0B; X-ray; 2.40 A; A/B=64-238.
DR PDBsum; 4Y0B; -.
DR AlphaFoldDB; Q93WL3; -.
DR SMR; Q93WL3; -.
DR IntAct; Q93WL3; 1.
DR STRING; 3702.AT4G25370.1; -.
DR MetOSite; Q93WL3; -.
DR PaxDb; Q93WL3; -.
DR PRIDE; Q93WL3; -.
DR ProteomicsDB; 220529; -.
DR EnsemblPlants; AT4G25370.1; AT4G25370.1; AT4G25370.
DR GeneID; 828640; -.
DR Gramene; AT4G25370.1; AT4G25370.1; AT4G25370.
DR KEGG; ath:AT4G25370; -.
DR Araport; AT4G25370; -.
DR TAIR; locus:2138048; AT4G25370.
DR eggNOG; ENOG502QSIB; Eukaryota.
DR HOGENOM; CLU_086193_1_0_1; -.
DR InParanoid; Q93WL3; -.
DR OMA; SKFLWAN; -.
DR OrthoDB; 1280014at2759; -.
DR PhylomeDB; Q93WL3; -.
DR PRO; PR:Q93WL3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93WL3; baseline and differential.
DR Genevisible; Q93WL3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009532; C:plastid stroma; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR Gene3D; 1.10.1780.10; -; 1.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR044217; CLPT1/2.
DR PANTHER; PTHR47016; PTHR47016; 1.
DR Pfam; PF02861; Clp_N; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR PROSITE; PS51903; CLP_R; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Plastid; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000305|PubMed:25921872"
FT CHAIN 65..238
FT /note="ATP-dependent Clp protease ATP-binding subunit
FT CLPT1, chloroplastic"
FT /id="PRO_0000434552"
FT DOMAIN 83..228
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 86..151
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 163..228
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT MUTAGEN 111
FT /note="T->V: No effect."
FT /evidence="ECO:0000269|PubMed:25921872"
FT MUTAGEN 153..156
FT /note="MYFF->AAAA: Loss of stabilization of ClpP and ClpR
FT ring interaction, but no effect on the interaction with the
FT ClpP ring."
FT /evidence="ECO:0000269|PubMed:25921872"
FT MUTAGEN 164
FT /note="T->V: No effect."
FT /evidence="ECO:0000269|PubMed:25921872"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:4Y0B"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4Y0B"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:4Y0B"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:4Y0B"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:4Y0B"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:4Y0B"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4Y0B"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:4Y0B"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:4Y0B"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:4Y0B"
SQ SEQUENCE 238 AA; 26050 MW; 0CE01964D04E9215 CRC64;
MASYTVSFIP LTLSNPRIFV SRQNGSPSSS SRIPLTSSLL GKKLLATQPS HRCFVPKLRC
LTSASTVLNV PIAQPENGSS DKIPKWSARA IKSLAMGELE ARKLKYPSTG TEAILMGILV
EGTSTVAKFL RGNGVTLFKV RDETLSLLGK SDMYFFSPEH PPLTEPAQKA IAWAIDEKNK
SDVDGELTTA YLLLGVWSQK DSAGRQILEK LGFNEDKAKE VEKSMNEDVD LSFKKQGQ
