ID   CLPP_CHLSC              Reviewed;         201 AA.
AC   A6MME7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
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   Chloranthus spicatus (Chulantree) (Nigrina spicata).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Chloranthales; Chloranthaceae; Chloranthus.
OX   NCBI_TaxID=13006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17644003; DOI=10.1016/j.ympev.2007.06.004;
RA   Hansen D.R., Dastidar S.G., Cai Z., Penaflor C., Kuehl J.V., Boore J.L.,
RA   Jansen R.K.;
RT   "Phylogenetic and evolutionary implications of complete chloroplast genome
RT   sequences of four early-diverging angiosperms: Buxus (Buxaceae),
RT   Chloranthus (Chloranthaceae), Dioscorea (Dioscoreaceae), and Illicium
RT   (Schisandraceae).";
RL   Mol. Phylogenet. Evol. 45:547-563(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.
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}.
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; EF380352; ABQ43284.1; -; Genomic_DNA.
DR   RefSeq; YP_001294123.1; NC_009598.1.
DR   AlphaFoldDB; A6MME7; -.
DR   SMR; A6MME7; -.
DR   MEROPS; S14.002; -.
DR   GeneID; 5236546; -.
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   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   3: Inferred from homology;
KW   Chloroplast; Hydrolase; Plastid; Protease; Serine protease.
FT   CHAIN           1..201
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000309293"
FT   ACT_SITE        100
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   201 AA;  22468 MW;  F06F0B5131A0307E CRC64;
     MPIGVPKVPF RSPGEEDAVW VDVNRLHRER LLFLGQEVDS EISNQLVGLM VYLSIEDDTR
     DLYLFINSPG GWVIPGLTIY DTMQFVPPDV HTICMGLAAS MGSFILVGGE ITKRLAFPHA
     RIMIHQPASS FYEAQAGEFI LEAEELLKLR ETLTRVYVQR TGNPLWIVSE DMERDVFMSA
     TEAQAHGIVD LVAVENTGDF A