ID   CLPP_CUSRE              Reviewed;         201 AA.
AC   A7M988;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
GN   Name=clpP;
OS   Cuscuta reflexa (Southern Asian dodder).
OG   Plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC   Cuscuta subgen. Monogynella.
OX   NCBI_TaxID=4129;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17714582; DOI=10.1186/1471-2229-7-45;
RA   Funk H.T., Berg S., Krupinska K., Maier U.-G., Krause K.;
RT   "Complete DNA sequences of the plastid genomes of two parasitic flowering
RT   plant species, Cuscuta reflexa and Cuscuta gronovii.";
RL   BMC Plant Biol. 7:45-45(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 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 plastid Clp protease core complex.
CC   -!- SUBCELLULAR LOCATION: Plastid.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
CC   -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC       some thylakoids, although the photosynthetic activity does not exceed
CC       the light compensation point. {ECO:0000305}.
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DR   EMBL; AM711640; CAM98416.1; -; Genomic_DNA.
DR   RefSeq; YP_001430129.1; NC_009766.1.
DR   AlphaFoldDB; A7M988; -.
DR   SMR; A7M988; -.
DR   MEROPS; S14.002; -.
DR   GeneID; 5536666; -.
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..201
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000309297"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   201 AA;  22593 MW;  9516268E8504A659 CRC64;
     MPIGVPRVRF QYRRDRSRVW IDIYNRLYRE RCLFLAHVVE SQIANQLVGL FIYLGVQDET
     KDIFLFINSP GGGIISGFAI YDTMQFVRPD IQTICVGLAA SMGSFLLVGG AITKRLAFPH
     ARVMIHQPMS AFFETQTVEA ILEAEELLKL RESLAKVYVQ RTGKPDWVIA EDMERDVFLS
     ATEAQSYGIV DVVGVALASK G