ID   CLPP_BIGNA              Reviewed;         195 AA.
AC   Q06J25;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
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   Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain
OS   CCMP621)).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Bigelowiella.
OX   NCBI_TaxID=227086;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16990439; DOI=10.1093/molbev/msl129;
RA   Rogers M.B., Gilson P.R., Su V., McFadden G.I., Keeling P.J.;
RT   "The complete chloroplast genome of the chlorarachniophyte Bigelowiella
RT   natans: evidence for independent origins of chlorarachniophyte and euglenid
RT   secondary endosymbionts.";
RL   Mol. Biol. Evol. 24:54-62(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   -!- 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; DQ851108; ABG91434.1; -; Genomic_DNA.
DR   RefSeq; YP_778602.1; NC_008408.1.
DR   AlphaFoldDB; Q06J25; -.
DR   SMR; Q06J25; -.
DR   MEROPS; S14.002; -.
DR   GeneID; 4353019; -.
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..195
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000295905"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   195 AA;  22355 MW;  77AFF6C810A6D2A1 CRC64;
     MPIGIPKVLF KESTDTTPQW VDIYTRLYKD RIIFLFQLLD DDFSNQIISM LLHLDSESKE
     ELIYFYINSV GGSVLSGISI YDTMNFINSE IVTLCIGIAS SISSLILANG KRTKRFILPH
     SRVLLHQPIM QVSGQASDIL IESEEILRLR RILTKIYIEN IDQTISRVAR DIDRDCFLSS
     REAKNYGIVD YILTN