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CLPP_ORYSJ
ID   CLPP_ORYSJ              Reviewed;         216 AA.
AC   P0C314; P12209; Q6QXZ5; Q6QY59;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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};
GN   OrderedLocusNames=LOC_Osp1g00590; ORFNames=Nip089;
OS   Oryza sativa subsp. japonica (Rice).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=2770692; DOI=10.1007/bf02464880;
RA   Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., Mori M.,
RA   Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., Kanno A.,
RA   Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.;
RT   "The complete sequence of the rice (Oryza sativa) chloroplast genome:
RT   intermolecular recombination between distinct tRNA genes accounts for a
RT   major plastid DNA inversion during the evolution of the cereals.";
RL   Mol. Gen. Genet. 217:185-194(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15122023; DOI=10.1104/pp.103.031245;
RA   Tang J., Xia H., Cao M., Zhang X., Zeng W., Hu S., Tong W., Wang J.,
RA   Wang J., Yu J., Yang H., Zhu L.;
RT   "A comparison of rice chloroplast genomes.";
RL   Plant Physiol. 135:412-420(2004).
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; X15901; CAA33972.1; -; Genomic_DNA.
DR   EMBL; AY522330; AAS46136.1; -; Genomic_DNA.
DR   PIR; JQ0251; JQ0251.
DR   RefSeq; NP_039410.1; NC_001320.1.
DR   AlphaFoldDB; P0C314; -.
DR   SMR; P0C314; -.
DR   BioGRID; 792842; 1.
DR   STRING; 39947.P0C314; -.
DR   MEROPS; S14.002; -.
DR   PaxDb; P0C314; -.
DR   PRIDE; P0C314; -.
DR   GeneID; 3131474; -.
DR   KEGG; osa:3131474; -.
DR   InParanoid; P0C314; -.
DR   OrthoDB; 1274502at2759; -.
DR   Proteomes; UP000059680; Chloroplast.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR   GO; GO:0009536; C:plastid; IC:Gramene.
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_0000288627"
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        60
FT                   /note="I -> S (in Ref. 1; CAA33972)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="D -> N (in Ref. 1; CAA33972)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="I -> T (in Ref. 1; CAA33972)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="A -> P (in Ref. 1; CAA33972)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   216 AA;  24728 MW;  B5286725D187763F CRC64;
     MPIGVPKVPY RIPGDEEATW VDLYNVMYRE RTLFLGQEIR CEVTNHITGL MVYLSIEDGI
     SDIFLFINSP GGWLISGMAI FDTMQTVTPD IYTICLGIAA SMASFILLGG EPTKRIAFPH
     ARIMLHQPAS AYYRARTPEF LLEVEELHKV REMITRVYAL RTGKPFWVVS EDMERDVFMS
     ADEAKAYGLV DIVGDEMLDE HCDTDPVWFP EMFKDW
 
 
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