CLPP_DRIGR
ID CLPP_DRIGR Reviewed; 202 AA.
AC Q06GX2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Drimys granadensis.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Canellales; Winteraceae; Drimys.
OX NCBI_TaxID=224735;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17020608; DOI=10.1186/1471-2148-6-77;
RA Cai Z., Penaflor C., Kuehl J.V., Leebens-Mack J., Carlson J.E.,
RA dePamphilis C.W., Boore J.L., Jansen R.K.;
RT "Complete plastid genome sequences of Drimys, Liriodendron, and Piper:
RT implications for the phylogenetic relationships of magnoliids.";
RL BMC Evol. Biol. 6:77-77(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.
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; DQ887676; ABH88321.1; -; Genomic_DNA.
DR RefSeq; YP_784411.1; NC_008456.1.
DR AlphaFoldDB; Q06GX2; -.
DR SMR; Q06GX2; -.
DR MEROPS; S14.002; -.
DR GeneID; 4363597; -.
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..202
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000275283"
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 202 AA; 22602 MW; A500D00345366958 CRC64;
MPIGVPKVPF RSPGEEDAVW VDVYNRLHRE RLLFLGQEVD SEISNQLVGL MVYLSIEDDT
RDLYLFINSP GGWVIPGIAI YDTMQFVPPD VHTICMGLAA SMGSFILVGG EITKRLAFPH
ARVMIHQPAS SFYEAPTGEF ILEAEELLKL RETLTRVYVQ RTGNPLWVIS EDMERDVFMS
ATEAQAHGIV DVVAVENTGD FT
