ID I0BRS6_9BACL Unreviewed; 196 AA. AC I0BRS6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 22-JAN-2014, entry version 12. DE RecName: Full=ATP-dependent Clp protease proteolytic subunit; DE EC=3.4.21.92; DE AltName: Full=Endopeptidase Clp; GN Name=clpP; ORFNames=B2K_30945; OS Paenibacillus mucilaginosus K02. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=997761; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K02; RA Xiao B., Sun L., Xiao L., Lian B.; RT "Complete genome sequence of Paenibacillus mucilaginosus K02."; RL Submitted (JUN-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 -!- SUBCELLULAR LOCATION: Cytoplasm (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; CP003422; AFH65073.1; -; Genomic_DNA. DR RefSeq; YP_006192838.1; NC_017672.3. DR EnsemblBacteria; AFH65073; AFH65073; B2K_30945. DR GeneID; 12734302; -. DR KEGG; pmw:B2K_30945; -. DR KO; K01358; -. DR BioCyc; PMUC997761:GLI6-6124-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; 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 TIGRFAMs; TIGR00493; clpP; 1. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase; KW Nucleotide-binding; Protease; Serine protease. FT ACT_SITE 98 98 By similarity. FT ACT_SITE 123 123 By similarity. SQ SEQUENCE 196 AA; 21462 MW; 9AFA59087989C59A CRC64; MTLVPMVVEQ EGRGERSYDI YSRLLKDRII FLGSAIDDDV ANLVIAQLLF LAATDPDKDI HLYINSPGGS VTAGMGIYDT MQFIKPDVST ICVGLAASMG SLLLTAGAPG KRFALPNSEV MIHQPLGGVR GQASDIKIHA DWIIKTKRKL NEIYVARTGQ PYDKIERDTD RDNFMSAAEA KEYGLIDAVI TRSDLT //