ID   CLPP_OENEH              Reviewed;         249 AA.
AC   Q9MTJ8;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
DE            EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE   AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
GN   Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444};
OS   Oenothera elata subsp. hookeri (Hooker's evening primrose) (Oenothera
OS   hookeri).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX   NCBI_TaxID=85636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Johansen;
RX   PubMed=10852478; DOI=10.1007/pl00008686;
RA   Hupfer H., Swiatek M., Hornung S., Herrmann R.G., Maier R.M., Chiu W.-L.,
RA   Sears B.;
RT   "Complete nucleotide sequence of the Oenothera elata plastid chromosome,
RT   representing plastome I of the five distinguishable Euoenothera
RT   plastomes.";
RL   Mol. Gen. Genet. 263:581-585(2000).
RN   [2]
RP   SEQUENCE REVISION TO 89 AND 94.
RX   PubMed=18299283; DOI=10.1093/nar/gkn081;
RA   Greiner S., Wang X., Rauwolf U., Silber M.V., Mayer K., Meurer J.,
RA   Haberer G., Herrmann R.G.;
RT   "The complete nucleotide sequences of the five genetically distinct plastid
RT   genomes of Oenothera, subsection Oenothera: I. Sequence evaluation and
RT   plastome evolution.";
RL   Nucleic Acids Res. 36:2366-2378(2008).
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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
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DR   EMBL; AJ271079; CAB67184.2; -; Genomic_DNA.
DR   RefSeq; NP_084718.2; NC_002693.2.
DR   AlphaFoldDB; Q9MTJ8; -.
DR   SMR; Q9MTJ8; -.
DR   MEROPS; S14.002; -.
DR   GeneID; 802828; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Chloroplast; Hydrolase; Plastid; Protease; Serine protease.
FT   CHAIN           1..249
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000179748"
FT   REGION          212..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   249 AA;  27956 MW;  6868965679DBAC0A CRC64;
     MPIGMPKIPF LLDGDEEDEE EDDATWVDLY NVLYRTRSIF LGDAIHFEVA NHIAGLMIFL
     TIQDATQNLY FFINSPGGLA VAGLLIYDTM QYVTPPVYTL GLGVLASMAS FLLVGGETSK
     RLMGPNGRVM IHQPESDYTH KDQSLEVQLD SGEVEDIRKM VIRVYLERTR LPREVLNDHL
     ERNYFMTATE AKYYGIVDDI GIQNLLARLR AESASQDNSL DPDAPDESAS QDNSLDPDAP
     DETRPPKLR