ID   CLPP_MARPO              Reviewed;         203 AA.
AC   P12208;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 104.
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   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3199436; DOI=10.1016/0022-2836(88)90003-4;
RA   Fukuzawa H., Kohchi T., Sano T., Shirai H., Umesono K., Inokuchi H.,
RA   Ozeki H., Ohyama K.;
RT   "Structure and organization of Marchantia polymorpha chloroplast genome.
RT   III. Gene organization of the large single copy region from rbcL to
RT   trnI(CAU).";
RL   J. Mol. Biol. 203:333-351(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1038/322572a0;
RA   Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA   Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT   "Chloroplast gene organization deduced from complete sequence of liverwort
RT   Marchantia polymorpha chloroplast DNA.";
RL   Nature 322:572-574(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 184-203.
RA   Fukuzawa H., Kohchi T., Shirai H., Ohyama K., Umesono K., Inokuchi H.,
RA   Ozeki H.;
RT   "Coding sequences for chloroplast ribosomal protein S12 from the liverwort,
RT   Marchantia polymorpha, are separated far apart on the different DNA
RT   strands.";
RL   FEBS Lett. 198:11-15(1986).
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   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
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DR   EMBL; X04465; CAA28109.1; -; Genomic_DNA.
DR   EMBL; X03661; CAA27296.1; -; Genomic_DNA.
DR   PIR; S01545; A05056.
DR   RefSeq; NP_039323.1; NC_001319.1.
DR   AlphaFoldDB; P12208; -.
DR   SMR; P12208; -.
DR   MEROPS; S14.002; -.
DR   GeneID; 2702606; -.
DR   BRENDA; 3.4.21.92; 3182.
DR   GO; GO:0009534; C:chloroplast thylakoid; IEA:EnsemblPlants.
DR   GO; GO:0009840; C:chloroplastic endopeptidase Clp complex; IEA:EnsemblPlants.
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   Chloroplast; Hydrolase; Plastid; Protease; Serine protease.
FT   CHAIN           1..203
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000179744"
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"
FT   CONFLICT        184
FT                   /note="A -> E (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  22685 MW;  C0C30114F13CB89B CRC64;
     MPIGVPKVPF RLPGEEDAVW IDVYNRLYRE RLLFLGQQVD DEIANQLIGI MMYLNGEDES
     KDMYLYINSP GGAVLAGISV YDAMQFVVPD VHTICMGLAA SMGSFILTGG EITKRIALPH
     ARVMIHQPAS SYYDGQAGEC IMEAEEVLKL RDCITKVYVQ RTGKPLWVIS EDMERDVFMS
     AKEAKLYGIV DLVAIENNST IKN