ID   CLPP_PINST              Reviewed;          80 AA.
AC   P84723; P84728;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Putative ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
DE   AltName: Full=PS7/PS12;
DE   Flags: Fragments;
GN   Name=clpP {ECO:0000250|UniProtKB:Q85X43};
OS   Pinus strobus (Eastern white pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Strobus.
OX   NCBI_TaxID=3348;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf {ECO:0000269|PubMed:16529377};
RX   PubMed=16529377; DOI=10.1094/mpmi-19-0150;
RA   Smith J.A., Blanchette R.A., Burnes T.A., Jacobs J.J., Higgins L.,
RA   Witthuhn B.A., David A.J., Gillman J.H.;
RT   "Proteomic comparison of needles from blister rust-resistant and
RT   susceptible Pinus strobus seedlings reveals upregulation of putative
RT   disease resistance proteins.";
RL   Mol. Plant Microbe Interact. 19:150-160(2006).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q85X43}.
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:0000250|UniProtKB:Q85X43,
CC         ECO:0000255|PROSITE-ProRule:PRU10085, ECO:0000255|PROSITE-
CC         ProRule:PRU10086};
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.7,
CC       its MW is: 22.8 kDa. {ECO:0000269|PubMed:16529377}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:16529377}.
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DR   AlphaFoldDB; P84723; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Hydrolase; Plastid; Protease;
KW   Serine protease.
FT   CHAIN           <1..>80
FT                   /note="Putative ATP-dependent Clp protease proteolytic
FT                   subunit"
FT                   /id="PRO_0000240627"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10085,
FT                   ECO:0000255|PROSITE-ProRule:PRU10086"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000305"
FT   NON_CONS        26..27
FT                   /evidence="ECO:0000305"
FT   NON_CONS        35..36
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        43..44
FT                   /evidence="ECO:0000305"
FT   NON_CONS        53..54
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        61..62
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        72..73
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         80
FT                   /evidence="ECO:0000303|PubMed:16529377"
SQ   SEQUENCE   80 AA;  8790 MW;  5109124F0341ABAB CRC64;
     APTEADATWV DLYNRVMIHQ PASSYYAAEM HNEAKTDNPE EVLDLDRDVF MSAAYGIVDT
     VWYVQAELVN GRGGAVVAGL