ID   CLPP_EPIVI              Reviewed;         196 AA.
AC   P30063;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
GN   Name=clpP;
OS   Epifagus virginiana (Beechdrops) (Orobanche virginiana).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Orobanchaceae; Orobancheae; Epifagus.
OX   NCBI_TaxID=4177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1332054; DOI=10.1073/pnas.89.22.10648;
RA   Wolfe K.H., Morden C.W., Palmer J.D.;
RT   "Function and evolution of a minimal plastid genome from a
RT   nonphotosynthetic parasitic plant.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10648-10652(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1404416; DOI=10.1007/bf00161168;
RA   Wolfe K.H., Morden C.W., Ems S.C., Palmer J.D.;
RT   "Rapid evolution of the plastid translational apparatus in a
RT   nonphotosynthetic plant: loss or accelerated sequence evolution of tRNA and
RT   ribosomal protein genes.";
RL   J. Mol. Evol. 35:304-317(1992).
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;
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
CC   -!- SUBCELLULAR LOCATION: Plastid.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR   EMBL; M81884; AAA65858.1; -; Genomic_DNA.
DR   PIR; S78388; S78388.
DR   RefSeq; NP_054384.1; NC_001568.1.
DR   AlphaFoldDB; P30063; -.
DR   SMR; P30063; -.
DR   MEROPS; S14.002; -.
DR   GeneID; 801415; -.
DR   BRENDA; 3.4.21.92; 6977.
DR   GO; GO:0009532; C:plastid stroma; IEA:UniProt.
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   Hydrolase; Plastid; Protease; Serine protease.
FT   CHAIN           1..196
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000179739"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   196 AA;  22110 MW;  5BBC4CAB96B68E6C CRC64;
     MPIGVPKVPF QIPGEEDASW VDVYNRLYRE RLLFLGQEVD SDISNQLIGL MVYLSIEDDT
     KEIYLFINSP GGWVIPGVAI YDTMQFVRPE VHTICMGLAA SMGSFLLVGG EITKRLAFPH
     ARVMIHQPAS YFFGAQTGEF ILEAEELLKL RETLTRVYVQ RTGKPLWVIS EDMERDVFMS
     AKDAQAYGIV DLVAVE