ID   CLPP_TUPAK              Reviewed;         198 AA.
AC   Q3ZJ12;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
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   Tupiella akineta (Green alga) (Pseudendoclonium akinetum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; OUU clade;
OC   Ulotrichales; Tupiellaceae; Tupiella.
OX   NCBI_TaxID=160070;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 1912;
RX   PubMed=15930151; DOI=10.1093/molbev/msi182;
RA   Pombert J.-F., Otis C., Lemieux C., Turmel M.;
RT   "The chloroplast genome sequence of the green alga Pseudendoclonium
RT   akinetum (Ulvophyceae) reveals unusual structural features and new insights
RT   into the branching order of chlorophyte lineages.";
RL   Mol. Biol. Evol. 22:1903-1918(2005).
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; AY835431; AAV80677.1; -; Genomic_DNA.
DR   RefSeq; YP_636255.1; NC_008114.1.
DR   AlphaFoldDB; Q3ZJ12; -.
DR   SMR; Q3ZJ12; -.
DR   MEROPS; S14.002; -.
DR   PRIDE; Q3ZJ12; -.
DR   GeneID; 4108749; -.
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   3: Inferred from homology;
KW   Chloroplast; Hydrolase; Plastid; Protease; Serine protease.
FT   CHAIN           1..198
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000275300"
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   198 AA;  21872 MW;  906E380C238ABAC1 CRC64;
     MPIGVPKVPY RLAGNEVAEW VDLYNRLYRE RVLFLCQDLD DELANQLIGI MLYLNAEDKS
     KGIYVYINSP GGSVTCGVGV FDAMNYIKSD VTTICVGTAA SMASFVLAGG RKGKRLALPH
     SRIMIHQPEG GSQGQASVVL SESEEVLRIR DEVAQIYSER TGQTLERISR DMNRDQFMSA
     REAKDYGLVD QIASSVSQ