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 03-APR-2013, entry version 36.
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; core eudicotyledons;
OC 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:HAMAP.
DR GO; GO:0006508; P:proteolysis; IEA: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
//
