CLPP_PHAAO
ID CLPP_PHAAO Reviewed; 204 AA.
AC Q3BAL3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 Phalaenopsis aphrodite subsp. formosana (Moth orchid).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Vandeae; Aeridinae; Phalaenopsis.
OX NCBI_TaxID=308872;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Taisugar TS-97;
RX PubMed=16207935; DOI=10.1093/molbev/msj029;
RA Chang C.-C., Lin H.-C., Lin I.-P., Chow T.-Y., Chen H.-H., Chen W.-H.,
RA Cheng C.-H., Lin C.-Y., Liu S.-M., Chang C.-C., Chaw S.-M.;
RT "The chloroplast genome of Phalaenopsis aphrodite (Orchidaceae):
RT comparative analysis of evolutionary rate with that of grasses and its
RT phylogenetic implications.";
RL Mol. Biol. Evol. 23:279-291(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY916449; AAW82524.1; -; Genomic_DNA.
DR RefSeq; YP_358605.1; NC_007499.1.
DR AlphaFoldDB; Q3BAL3; -.
DR SMR; Q3BAL3; -.
DR MEROPS; S14.002; -.
DR GeneID; 3741705; -.
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..204
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000275297"
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 204 AA; 22925 MW; 3476CF2DA77E88AA CRC64;
MPIGVPKVPF RNPGEEDAVW VDVYNRLHRE RLLFLGQEVD SEISNQIVGL MVYLSIEDDT
RDLYLFINSP GGWVIPGIAI YDTMQFVLPD VHTICMGLAA SMGSFILVGG EITKRLAFPH
ARVMIHQPAS SFYEAQARDF ILEAEELLKL RETLTKVYVQ RTGNPLWVIS EDMERDVFMS
ATEAQAHGIV DLVAIENENT GNSI
