ID I0BRS6_9BACL Unreviewed; 196 AA. AC I0BRS6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 13-SEP-2023, entry version 56. 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 ORFNames=B2K_30945 {ECO:0000313|EMBL:AFH65073.1}; OS Paenibacillus mucilaginosus K02. OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH65073.1, ECO:0000313|Proteomes:UP000007392}; RN [1] {ECO:0000313|EMBL:AFH65073.1, ECO:0000313|Proteomes:UP000007392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K02 {ECO:0000313|EMBL:AFH65073.1, RC ECO:0000313|Proteomes:UP000007392}; 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. CC {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU000550}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins to small peptides in the presence of CC ATP and magnesium. alpha-casein is the usual test substrate. In the CC absence of ATP, only oligopeptides shorter than five residues are CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr- CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also CC occurs).; EC=3.4.21.92; Evidence={ECO:0000256|ARBA:ARBA00034021, CC ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|PROSITE- CC ProRule:PRU10086}; CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which CC stack back to back to give a disk-like structure with a central cavity, CC resembling the structure of eukaryotic proteasomes. {ECO:0000256|HAMAP- CC Rule:MF_00444}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444}. CC -!- SIMILARITY: Belongs to the peptidase S14 family. CC {ECO:0000256|ARBA:ARBA00007039, ECO:0000256|HAMAP-Rule:MF_00444, CC 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; CP003422; AFH65073.1; -; Genomic_DNA. DR RefSeq; WP_013920148.1; NC_017672.3. DR AlphaFoldDB; I0BRS6; -. DR MEROPS; S14.001; -. DR EnsemblBacteria; AFH65073; AFH65073; B2K_30945. DR KEGG; pmw:B2K_30945; -. DR PATRIC; fig|997761.3.peg.6195; -. DR HOGENOM; CLU_058707_3_2_9; -. DR OrthoDB; 9802800at2; -. DR Proteomes; UP000007392; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule. DR CDD; cd07017; S14_ClpP_2; 1. DR HAMAP; MF_00444; ClpP; 1. DR InterPro; IPR001907; ClpP. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR023562; ClpP/TepA. DR InterPro; IPR033135; ClpP_His_AS. DR InterPro; IPR018215; ClpP_Ser_AS. DR NCBIfam; TIGR00493; clpP; 1. DR PANTHER; PTHR10381; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1. DR PANTHER; PTHR10381:SF70; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1. DR Pfam; PF00574; CLP_protease; 1. DR PRINTS; PR00127; CLPPROTEASEP. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00444}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00444}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP- KW Rule:MF_00444}. FT ACT_SITE 98 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10085" FT ACT_SITE 98 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00444" FT ACT_SITE 123 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00444, FT ECO:0000256|PROSITE-ProRule:PRU10086" 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 //