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