CLPP_WHEAT
ID CLPP_WHEAT Reviewed; 216 AA.
AC P24064;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 120.
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 Triticum aestivum (Wheat).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Mardler;
RX PubMed=2103485; DOI=10.1007/bf00039435;
RA Gray J.C., Hird S.M., Dyer T.A.;
RT "Nucleotide sequence of a wheat chloroplast gene encoding the proteolytic
RT subunit of an ATP-dependent protease.";
RL Plant Mol. Biol. 15:947-950(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T.,
RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., Gojobori T.,
RA Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., Tsunewaki K.;
RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: complete
RT sequence and contig clones.";
RL Plant Mol. Biol. Rep. 18:243-253(2000).
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; X54484; CAA38354.1; -; Genomic_DNA.
DR EMBL; AB042240; BAB47058.1; -; Genomic_DNA.
DR PIR; S12408; S12408.
DR RefSeq; NP_114282.1; NC_002762.1.
DR AlphaFoldDB; P24064; -.
DR SMR; P24064; -.
DR STRING; 4565.EPlTAEP00000010075; -.
DR MEROPS; S14.002; -.
DR PRIDE; P24064; -.
DR GeneID; 803203; -.
DR KEGG; taes:803203; -.
DR eggNOG; KOG0840; Eukaryota.
DR HOGENOM; CLU_058707_4_2_1; -.
DR BRENDA; 3.4.21.92; 6500.
DR Proteomes; UP000019116; Chloroplast.
DR ExpressionAtlas; P24064; baseline.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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; Reference proteome;
KW Serine protease.
FT CHAIN 1..216
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179761"
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"
FT CONFLICT 14
FT /note="G -> R (in Ref. 1; CAA38354)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="I -> R (in Ref. 1; CAA38354)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="F -> S (in Ref. 1; CAA38354)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="G -> E (in Ref. 1; CAA38354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24727 MW; B090604E70E4F439 CRC64;
MPIGVPKVPY RIPGDEEATW VDLYNVMYRE RTLFLGQEIR CEITNHITGL MVYLSIEDGI
SDIFLFINSP GGWLISGMAI FDTMQTVTPD IYTICLGIAA SMASFILLGG EPTKRIAFPH
ARIMLHQPAS AYYRARTPEF LLEVEELHKV REMITRVYAV RTGKPFWVVS EDMERDVFMS
ADEAKAYGLV DIVGDEMIDK HCDTDPVWFP EMFKDW
