CLPS1_ARATH
ID CLPS1_ARATH Reviewed; 159 AA.
AC Q9SX29; A8MS26;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ATP-dependent Clp protease adapter protein CLPS1, chloroplastic {ECO:0000303|Ref.6};
DE Flags: Precursor;
GN Name=CPLS1 {ECO:0000303|Ref.6};
GN Synonyms=CLPT {ECO:0000303|PubMed:14593120};
GN OrderedLocusNames=At1g68660 {ECO:0000312|Araport:AT1G68660};
GN ORFNames=F24J5.10 {ECO:0000312|EMBL:AAD49977.1},
GN F24J5.4 {ECO:0000312|EMBL:AAK73973.1};
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;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 1).
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] (ISOFORM 1).
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 NOMENCLATURE.
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 [6]
RP NOMENCLATURE, AND DISRUPTION PHENOTYPE.
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 [7]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION
RP WITH CLPC1; CLPC2; CLPT1 AND CLPT2, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF ASP-89 AND ASN-90.
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 [8]
RP FUNCTION, INTERACTION WITH CLPF, AND MUTAGENESIS OF 89-ASP-ASN-90.
RX PubMed=26419670; DOI=10.1105/tpc.15.00574;
RA Nishimura K., Apitz J., Friso G., Kim J., Ponnala L., Grimm B.,
RA van Wijk K.J.;
RT "Discovery of a unique Clp Component, ClpF, in chloroplasts: A proposed
RT binary ClpF-ClpS1 adaptor complex functions in substrate recognition and
RT delivery.";
RL Plant Cell 27:2677-2691(2015).
CC -!- FUNCTION: Small adapter protein that modulate the activity of CLPC (By
CC similarity). Involved in plastid biogenesis in particular when
CC chloroplast protein synthesis capacity is a limiting factor
CC (PubMed:23898032). Probably involved in substrate selection for plastid
CC Clp protease system (PubMed:23898032). Recruitment to ClpC chaperones
CC is facilitated by CLPF thus forming a binary adapter for selective
CC substrate recognition and delivery to plastid Clp protease system
CC (CLPC) (PubMed:26419670). {ECO:0000250|UniProtKB:P0A8Q6,
CC ECO:0000269|PubMed:23898032, ECO:0000269|PubMed:26419670}.
CC -!- SUBUNIT: Interacts with CLPC1 (via N-terminus) and CLPC2, but not with
CC CLPt1 or CLPT2 (PubMed:23898032). Binds to ClpF; this interaction
CC stimulates their association with ClpC (PubMed:26419670).
CC {ECO:0000269|PubMed:23898032, ECO:0000269|PubMed:26419670}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:23898032}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SX29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SX29-2; Sequence=VSP_057948;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in photosynthetic green
CC tissues with high levels in young, developing leaf tissues.
CC {ECO:0000269|PubMed:23898032}.
CC -!- DEVELOPMENTAL STAGE: Not detected in senescing leaves.
CC {ECO:0000269|PubMed:23898032}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (Ref.6, PubMed:23898032).
CC Weak chloroplast phenotype under short-day conditions
CC (PubMed:23898032). {ECO:0000269|PubMed:23898032, ECO:0000303|Ref.6}.
CC -!- SIMILARITY: Belongs to the ClpS family. {ECO:0000305}.
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DR EMBL; AC008075; AAD49977.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34824.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34825.1; -; Genomic_DNA.
DR EMBL; AF336921; AAG54002.1; -; mRNA.
DR EMBL; AY045615; AAK73973.1; -; mRNA.
DR EMBL; AY120696; AAM52239.1; -; mRNA.
DR EMBL; AY085795; AAM63011.1; -; mRNA.
DR PIR; B96711; B96711.
DR RefSeq; NP_001077794.1; NM_001084325.1. [Q9SX29-2]
DR RefSeq; NP_564937.1; NM_105538.3. [Q9SX29-1]
DR PDB; 7D34; X-ray; 2.01 A; A/B=79-159.
DR PDBsum; 7D34; -.
DR AlphaFoldDB; Q9SX29; -.
DR SMR; Q9SX29; -.
DR STRING; 3702.AT1G68660.1; -.
DR PaxDb; Q9SX29; -.
DR PRIDE; Q9SX29; -.
DR ProteomicsDB; 246661; -. [Q9SX29-1]
DR EnsemblPlants; AT1G68660.1; AT1G68660.1; AT1G68660. [Q9SX29-1]
DR EnsemblPlants; AT1G68660.2; AT1G68660.2; AT1G68660. [Q9SX29-2]
DR GeneID; 843196; -.
DR Gramene; AT1G68660.1; AT1G68660.1; AT1G68660. [Q9SX29-1]
DR Gramene; AT1G68660.2; AT1G68660.2; AT1G68660. [Q9SX29-2]
DR KEGG; ath:AT1G68660; -.
DR Araport; AT1G68660; -.
DR TAIR; locus:2026869; AT1G68660.
DR eggNOG; ENOG502RZXT; Eukaryota.
DR HOGENOM; CLU_134083_1_0_1; -.
DR InParanoid; Q9SX29; -.
DR OMA; ETAICSR; -.
DR PhylomeDB; Q9SX29; -.
DR PRO; PR:Q9SX29; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SX29; baseline and differential.
DR Genevisible; Q9SX29; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:TAIR.
DR GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; IDA:TAIR.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR022935; ClpS.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR PANTHER; PTHR33473; PTHR33473; 1.
DR Pfam; PF02617; ClpS; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Hydrolase; Plastid;
KW Protease; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..159
FT /note="ATP-dependent Clp protease adapter protein CLPS1,
FT chloroplastic"
FT /id="PRO_0000434551"
FT VAR_SEQ 104..133
FT /note="Missing (in isoform 2)"
FT /id="VSP_057948"
FT MUTAGEN 89..90
FT /note="DN->AA: Impaired interaction with CLPF."
FT /evidence="ECO:0000269|PubMed:26419670"
FT MUTAGEN 89
FT /note="D->A: Loss of interactions with some potential
FT substrates."
FT /evidence="ECO:0000269|PubMed:23898032"
FT MUTAGEN 90
FT /note="N->A: Loss of interactions with some potential
FT substrates."
FT /evidence="ECO:0000269|PubMed:23898032"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:7D34"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:7D34"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:7D34"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:7D34"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:7D34"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:7D34"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:7D34"
SQ SEQUENCE 159 AA; 17001 MW; E1D0AF6A32FD54FD CRC64;
METAICGRLA LAPSSLFNSK SGDKHLVSKG PCVNRSILMT LSTSAALGKG GGVLDKPIIE
KTTPGRESEF DLRKSKKIAP PYRVILHNDN FNKREYVVQV LMKVIPGMTV DNAVNIMQEA
HINGLAVVIV CAQADAEQHC MQLRGNGLLS SVEPDGGGC
