ID   CLPP_ADICA              Reviewed;         200 AA.
AC   Q85FJ8;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 74.
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   Adiantum capillus-veneris (Maidenhair fern).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC   Vittarioideae; Adiantum.
OX   NCBI_TaxID=13818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA   Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT   "Complete nucleotide sequence of the chloroplast genome from a
RT   leptosporangiate fern, Adiantum capillus-veneris L.";
RL   DNA Res. 10:59-65(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC   TISSUE=Frond;
RX   PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA   Wolf P.G., Rowe C.A., Hasebe M.;
RT   "High levels of RNA editing in a vascular plant chloroplast genome:
RT   analysis of transcripts from the fern Adiantum capillus-veneris.";
RL   Gene 339:89-97(2004).
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   -!- RNA EDITING: Modified_positions=65 {ECO:0000269|PubMed:15363849}, 105
CC       {ECO:0000269|PubMed:15363849}, 107 {ECO:0000269|PubMed:15363849}, 147
CC       {ECO:0000269|PubMed:15363849}, 148 {ECO:0000269|PubMed:15363849}, 190
CC       {ECO:0000269|PubMed:15363849};
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
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DR   EMBL; AY178864; AAP29415.2; -; Genomic_DNA.
DR   RefSeq; NP_848084.2; NC_004766.1.
DR   AlphaFoldDB; Q85FJ8; -.
DR   SMR; Q85FJ8; -.
DR   MEROPS; S14.002; -.
DR   GeneID; 807394; -.
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   2: Evidence at transcript level;
KW   Chloroplast; Hydrolase; Plastid; Protease; RNA editing; Serine protease.
FT   CHAIN           1..200
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000179731"
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   200 AA;  22282 MW;  113A64EC7BF53EA2 CRC64;
     MPIGVPKVPF RLPGEEDAVW VDVYNRLYRE RLLFLGQQVD DEIANQLIGI MMYLNSEDQA
     KDMYLYVNSP GGAVLAGISV YDAMQFVVPD VHTICMGLAA SMGSFILAGG EITRRIALPH
     ARVMIHQPAS SYYDGQAGEC VMEAEEVLKL RDCITKVYAQ RTGKPLWLIS EDMERDVFLS
     AEEAQDYGVV DLVAVENVSR