ID R9ZSL3_9FABA Unreviewed; 196 AA. AC R9ZSL3; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 19-FEB-2014, entry version 5. 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. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 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 //