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Database: UniProt
Entry: Q09MF2
LinkDB: Q09MF2
Original site: Q09MF2 
ID   CLPP_CITSI              Reviewed;         196 AA.
AC   Q09MF2;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   19-FEB-2014, entry version 38.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
GN   Name=clpP;
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Sapindales; Rutaceae; Citrus.
OX   NCBI_TaxID=2711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Osbeck var. Ridge Pineapple;
RX   PubMed=17010212; DOI=10.1186/1471-2229-6-21;
RA   Bausher M.G., Singh N.D., Lee S.-B., Jansen R.K., Daniell H.;
RT   "The complete chloroplast genome sequence of Citrus sinensis (L.)
RT   Osbeck var 'Ridge Pineapple': organization and phylogenetic
RT   relationships to other angiosperms.";
RL   BMC Plant Biol. 6:21-21(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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
CC       the presence of ATP and magnesium. Alpha-casein is the usual test
CC       substrate. In the absence of ATP, only oligopeptides shorter than
CC       five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
CC       and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu-
CC       and -Tyr-|-Trp bonds also occurs).
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
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DR   EMBL; DQ864733; ABI49044.1; -; Genomic_DNA.
DR   RefSeq; YP_740501.1; NC_008334.1.
DR   ProteinModelPortal; Q09MF2; -.
DR   MEROPS; S14.002; -.
DR   GeneID; 4271124; -.
DR   ProtClustDB; CHL00028; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00444; ClpP; 1.
DR   InterPro; IPR001907; ClpP.
DR   InterPro; IPR023562; ClpP/TepA.
DR   InterPro; IPR018215; ClpP_AS.
DR   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Hydrolase; Nucleotide-binding; Plastid;
KW   Protease; Serine protease.
FT   CHAIN         1    196       ATP-dependent Clp protease proteolytic
FT                                subunit.
FT                                /FTId=PRO_0000275279.
FT   ACT_SITE    101    101       By similarity.
FT   ACT_SITE    126    126       By similarity.
SQ   SEQUENCE   196 AA;  21912 MW;  F5FFCCEA72EC6DCF CRC64;
     MPIGVPKVPY RSPGDKHPSW VDIYNRLYRE RLLFLGQMVE SDISNQLIGI MVYLSIENET
     KDLYLFINSP GGWVIPGIAI YDTMQFVRPD VQTICMGLAA SMGSFLLAAG ASTKRLAFPH
     ARVMIHQPIG AFYGAQTGEF ILDTEELLRL REILTMVYVQ RSGKPLWVVS EDMERDTFMS
     ATEAQAHGLV DLVAVG
//
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