ID   R9ZSL3_9FABA            Unreviewed;       196 AA.
AC   R9ZSL3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   14-MAY-2014, entry version 7.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
GN   Name=clpP;
OS   Glycine stenophita.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   Phaseoleae; Glycine; Glycine.
OX   NCBI_TaxID=96944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Sherman-Broyles S., Bombarely A., Grimwood J., Schmutz J., Jackson S.,
RA   Doyle J.;
RT   "Comparative analysis of complete chloroplast sequences from seven
RT   perennial wild relatives of Glycine max.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- 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-and
CC       -Tyr-|-Trp bonds also occurs).
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
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DR   EMBL; KC893634; AGO44347.1; -; Genomic_DNA.
DR   RefSeq; YP_008145816.1; NC_021646.1.
DR   GeneID; 16793779; -.
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   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   ACT_SITE    101    101       By similarity.
FT   ACT_SITE    126    126       By similarity.
SQ   SEQUENCE   196 AA;  22106 MW;  68A8F3B77F947AEC CRC64;
     MPIGVPRVPF RSPGEEDASW VDIYNRLYRE RLLFLGQEVD SEISNQLISL MVYLSIEEEN
     KDLYLFINSP GGWVIPGIAI YDTMQFVQPD VQTVCMGLAA SMGSFLLAGG EITKRLAFPH
     ARVMIHQPAS SFYEAQTGEF ILEAEELLKM RETITRVYVQ RTGKPLWVIS EDMERDVFMS
     AAEAQAHGIV DLVAVE
//