CLPP_CHLRE
ID CLPP_CHLRE Reviewed; 524 AA.
AC P42380; B7U1F0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE EC=3.4.21.92;
DE AltName: Full=Endopeptidase Clp;
GN Name=clpP;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=137c / CC-125;
RX PubMed=8052234; DOI=10.1007/bf00283516;
RA Huang C., Wang S., Chen L., Lemieux C., Otis C., Turmel M., Liu X.-Q.;
RT "The Chlamydomonas chloroplast clpP gene contains translated large
RT insertion sequences and is essential for cell growth.";
RL Mol. Gen. Genet. 244:151-159(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [3]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
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 (By similarity).
CC {ECO:0000250}.
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|PROSITE-
CC ProRule:PRU10085, ECO:0000255|PROSITE-ProRule:PRU10086};
CC -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC -!- DOMAIN: This gene contains one large insertion sequence (IS1) that
CC divides the clpP gene into two sequence domains. The insertion sequence
CC forms a continuous open reading frame with its upstream and downstream
CC sequence domains.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR EMBL; L28803; AAA53086.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50097.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00910.1; -; Genomic_DNA.
DR PIR; T07988; T07988.
DR RefSeq; NP_958364.1; NC_005353.1.
DR PDB; 7EKO; EM; 3.30 A; H/J/M=317-524.
DR PDB; 7EKQ; EM; 3.60 A; H/J/M=317-524.
DR PDBsum; 7EKO; -.
DR PDBsum; 7EKQ; -.
DR AlphaFoldDB; P42380; -.
DR SMR; P42380; -.
DR STRING; 3055.DAA00910; -.
DR PaxDb; P42380; -.
DR PRIDE; P42380; -.
DR GeneID; 2717015; -.
DR KEGG; cre:ChreCp007; -.
DR eggNOG; KOG0840; Eukaryota.
DR HOGENOM; CLU_520112_0_0_1; -.
DR InParanoid; P42380; -.
DR OrthoDB; 1274502at2759; -.
DR BRENDA; 3.4.21.92; 1318.
DR Proteomes; UP000006906; Chloroplast.
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 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 3D-structure; Chloroplast; Hydrolase; Plastid; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..524
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179737"
FT REGION 60..345
FT /note="Insertion IS1"
FT REGION 74..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10085,
FT ECO:0000255|PROSITE-ProRule:PRU10086"
FT ACT_SITE 412
FT /evidence="ECO:0000250"
FT VARIANT 290
FT /note="R -> Q (in strain: CC-503)"
FT STRAND 348..356
FT /evidence="ECO:0007829|PDB:7EKO"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:7EKO"
FT STRAND 373..385
FT /evidence="ECO:0007829|PDB:7EKO"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:7EKO"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:7EKO"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:7EKO"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:7EKO"
FT HELIX 422..447
FT /evidence="ECO:0007829|PDB:7EKO"
FT HELIX 451..457
FT /evidence="ECO:0007829|PDB:7EKO"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:7EKO"
FT HELIX 466..472
FT /evidence="ECO:0007829|PDB:7EKO"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:7EKO"
FT HELIX 494..509
FT /evidence="ECO:0007829|PDB:7EKO"
SQ SEQUENCE 524 AA; 59501 MW; ACF82676C1D96813 CRC64;
MPIGVPRIIY CWGEELPAQW TDIYNFIFRR RMVFLMQYLD DELCNQICGL LINIHMEDRS
KELEKKEMEK SGLFKSGTAK TKGKDTVKKE NLSGGASAKR QSVEDLLTSD NDFGIEENHL
LEQYTLQKIT TEWLNWNAQF FDYSDEPYLY YLADILSKDF SPNQDKDSAN LNFAKSSANK
QAFQNPAEMT KLIKNLKNLK NFSTGSKNVK QNLDVYSPFR LLANFAPQNY NLEHPNQNLA
EIYSLLKTST QNTNQPFTKK LIDNLSHKEL MNRLQSPEKL VASSEKALGR RRLKQRYVQE
RLGSGGLSNS KALKAYNYLD QGALNNESGR SLYRKQTERV IQEEESKKVF MIINSFGGSV
GNGITVHDAL QFIKAGSLTL ALGVAASAAS LALAGGTIGE RYVTEGCHTM IHQPEGGLNG
QASDIWIDSQ EIMKIRLDVA EIYSLSTYRP RHKILRDLDR DFYLTAMETI YYGLADEIAT
NEVMHSIVEM TNQVWSYHDS KQERLLESRA SLVGDSTQTQ ESNS
