ID   CLPP_ANTAG              Reviewed;         204 AA.
AC   Q85BZ1;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
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   Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC   Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC   Anthoceros.
OX   NCBI_TaxID=48387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX   PubMed=12527781; DOI=10.1093/nar/gkg155;
RA   Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT   "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT   chloroplast genome: insight into the earliest land plants.";
RL   Nucleic Acids Res. 31:716-721(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC   TISSUE=Thallus;
RX   PubMed=12711687; DOI=10.1093/nar/gkg327;
RA   Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT   "RNA editing in hornwort chloroplasts makes more than half the genes
RT   functional.";
RL   Nucleic Acids Res. 31:2417-2423(2003).
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=20 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 34 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 37 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 69 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 93 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 105 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 106 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 148 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 173 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 189 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}, 190 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687}; Note=The nonsense codon at position 37 is
CC       modified to a sense codon.;
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; AB086179; BAC55373.1; -; Genomic_DNA.
DR   EMBL; AB087461; BAC55470.1; -; mRNA.
DR   RefSeq; NP_777437.1; NC_004543.1.
DR   AlphaFoldDB; Q85BZ1; -.
DR   SMR; Q85BZ1; -.
DR   MEROPS; S14.002; -.
DR   GeneID; 2553490; -.
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..204
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000179733"
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   204 AA;  22819 MW;  4E50E7E65B66A1E8 CRC64;
     MPIGVPKVPF RLPGEEDAVW IDVYNRLYRE RLLFLGQHVD DEIANQLIGI MMYLNGEDES
     KDMYLYINSP GGAVLAGISV YDTMQFVVPD VHTICMGLAA SMGSFILTGG EITKRIALPH
     ARIMIHQPAS SYYDGQAGEC IMEAEEVLKL RDCITKVYVQ RTGKPLWVIS EDMERDVFMS
     AKEAQIYGIV DFVAIETTSN SLTN