ID A0A097KNX2_9CHLO Unreviewed; 195 AA. AC A0A097KNX2; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 15-FEB-2017, entry version 9. DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU003567}; DE EC=3.4.21.92 {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU000549}; DE AltName: Full=Endopeptidase Clp {ECO:0000256|HAMAP-Rule:MF_00444}; GN Name=clpP {ECO:0000256|HAMAP-Rule:MF_00444, GN ECO:0000313|EMBL:AIT94909.1}; OS Paradoxia multiseta. OG Plastid; Chloroplast {ECO:0000313|EMBL:AIT94909.1}. OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; OC Trebouxiophyceae incertae sedis; Paradoxia. OX NCBI_TaxID=249350 {ECO:0000313|EMBL:AIT94909.1}; RN [1] {ECO:0000313|EMBL:AIT94909.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25270575; DOI=10.1186/s12862-014-0211-2; RA Lemieux C., Otis C., Turmel M.; RT "Chloroplast phylogenomic analysis resolves deep-level relationships RT within the green algal class Trebouxiophyceae."; RL BMC Evol. Biol. 14:211-211(2014). 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:0000256|HAMAP-Rule:MF_00444}. 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). {ECO:0000256|HAMAP- CC Rule:MF_00444, ECO:0000256|PROSITE-ProRule:PRU10086, CC ECO:0000256|RuleBase:RU000549}. CC -!- SUBUNIT: Component of the chloroplastic Clp protease core complex. CC {ECO:0000256|HAMAP-Rule:MF_00444}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma CC {ECO:0000256|HAMAP-Rule:MF_00444}. CC -!- SIMILARITY: Belongs to the peptidase S14 family. CC {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU003567}. 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; KM462879; AIT94909.1; -; Genomic_DNA. DR RefSeq; YP_009106142.1; NC_025540.1. DR GeneID; 22160296; -. DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_00444; ClpP; 1. DR InterPro; IPR001907; ClpP. DR InterPro; IPR029045; ClpP/crotonase-like_dom. 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 {ECO:0000313|EMBL:AIT94909.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00444, KW ECO:0000256|RuleBase:RU000549}; KW Plastid {ECO:0000313|EMBL:AIT94909.1}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00444, KW ECO:0000256|RuleBase:RU000549, ECO:0000313|EMBL:AIT94909.1}; KW Serine protease {ECO:0000256|HAMAP-Rule:MF_00444, KW ECO:0000256|RuleBase:RU000549}. FT ACT_SITE 101 101 {ECO:0000256|PROSITE-ProRule:PRU10085}. FT ACT_SITE 101 101 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_00444}. FT ACT_SITE 126 126 {ECO:0000256|HAMAP-Rule:MF_00444, FT ECO:0000256|PROSITE-ProRule:PRU10086}. SQ SEQUENCE 195 AA; 21636 MW; 46FF2697FC58D3BC CRC64; MPIGVPKVPF RLPGEPTAQW VDLYNRLYRE RVLFLCQELD DELANQLIGI MLYLNAEEKS KGLYIYINSP GGSVTCGIAV YDSMNYVKAD VTTICVGTAA SMASFVLAGG DRGKRIALPH SRIMIHQPEG GSQGQASEVL SESSEVMRIR RQVGKIYAER TGQPLSRISR DMDRDQFMSA REAKEYGLVD QVAVE //