ID   CLPP_OSTTA              Reviewed;         200 AA.
AC   Q0P3P4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   01-MAY-2013, entry version 41.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
GN   Name=clpP; OrderedLocusNames=OtCpg00080;
OS   Ostreococcus tauri.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Ostreococcus.
OX   NCBI_TaxID=70448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595;
RX   PubMed=17251180; DOI=10.1093/molbev/msm012;
RA   Robbens S., Derelle E., Ferraz C., Wuyts J., Moreau H.,
RA   Van de Peer Y.;
RT   "The complete chloroplast and mitochondrial DNA sequence of
RT   Ostreococcus tauri: organelle genomes of the smallest eukaryote are
RT   examples of compaction.";
RL   Mol. Biol. Evol. 24:956-968(2007).
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
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
CC       the presence of ATP and magnesium. Alpha-casein is the usual test
CC       substrate. In the absence of ATP, only oligopeptides shorter than
CC       five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
CC       and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu-
CC       and -Tyr-|-Trp bonds also occurs).
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
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DR   EMBL; CR954199; CAL36333.1; -; Genomic_DNA.
DR   RefSeq; YP_717211.1; NC_008289.1.
DR   ProteinModelPortal; Q0P3P4; -.
DR   STRING; 70448.Q0P3P4; -.
DR   MEROPS; S14.002; -.
DR   PRIDE; Q0P3P4; -.
DR   GeneID; 4238814; -.
DR   KEGG; ota:OstapCp08; -.
DR   eggNOG; COG0740; -.
DR   HOGENOM; HOG000285833; -.
DR   KO; K01358; -.
DR   ProtClustDB; CHL00028; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:HAMAP.
DR   HAMAP; MF_00444; ClpP; 1; -.
DR   InterPro; IPR001907; ClpP.
DR   InterPro; IPR023562; ClpP/TepA.
DR   InterPro; IPR018215; ClpP_AS.
DR   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Complete proteome; Hydrolase;
KW   Nucleotide-binding; Plastid; Protease; Serine protease.
FT   CHAIN         1    200       ATP-dependent Clp protease proteolytic
FT                                subunit.
FT                                /FTId=PRO_0000275295.
FT   ACT_SITE    101    101       By similarity.
FT   ACT_SITE    126    126       By similarity.
SQ   SEQUENCE   200 AA;  21871 MW;  78DC5BA1BBB0DE33 CRC64;
     MPIGVPKVAY RLPGESTPQW VDLYNRLYRE RVLFLGSGLD DELANQLNGI MLYLSAEDAS
     RSLFLYINSP GGSVTAGLSV FDIMNYVQAS VTTIGIGFAA SMASFILAGG ERGSRIALPH
     CRVMIHQPQG GMEGQASEVV LEKEEIVRLR RLIGRLYVDL TGQPLSTIAN DLDRDKYLSA
     REAREYGLVD LVATTETATV
//