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CLPPH_POPEU
ID   CLPPH_POPEU             Reviewed;          22 AA.
AC   P84982;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Probable ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
DE   Flags: Fragments;
OS   Populus euphratica (Euphrates poplar).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=75702;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf {ECO:0000269|Ref.1};
RA   Ferreira S.;
RT   "Molecular analysis of Populus euphratica Oliv. response to moderate heat
RT   stress.";
RL   Thesis (2006), ICAT-FCUL, Portugal.
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:Q3MDK7}.
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:Q3MDK7,
CC         ECO:0000255|PROSITE-ProRule:PRU10085, ECO:0000255|PROSITE-
CC         ProRule:PRU10086};
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255}.
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DR   AlphaFoldDB; P84982; -.
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   Direct protein sequencing; Hydrolase; Protease; Serine protease.
FT   CHAIN           <1..>22
FT                   /note="Probable ATP-dependent Clp protease proteolytic
FT                   subunit"
FT                   /id="PRO_0000307115"
FT   NON_CONS        11..12
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         22
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   22 AA;  2450 MW;  76441B1EB330A900 CRC64;
     IALQSPAGAA RIRDYLYNEL SK
 
 
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