ID A0A2M7B5X6_9BACT Unreviewed; 194 AA. AC A0A2M7B5X6; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 24-JAN-2024, entry version 14. 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}; DE AltName: Full=Endopeptidase Clp {ECO:0000256|HAMAP-Rule:MF_00444}; GN Name=clpP {ECO:0000256|HAMAP-Rule:MF_00444, GN ECO:0000313|EMBL:PIU98472.1}; GN ORFNames=COS61_01230 {ECO:0000313|EMBL:PIU98472.1}; OS Candidatus Wolfebacteria bacterium CG03_land_8_20_14_0_80_40_12. OC Bacteria; Candidatus Wolfebacteria. OX NCBI_TaxID=1975069 {ECO:0000313|EMBL:PIU98472.1, ECO:0000313|Proteomes:UP000228949}; RN [1] {ECO:0000313|Proteomes:UP000228949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.K., RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M., RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.; RT "Depth-based differentiation of microbial function through sediment-hosted RT aquifers and enrichment of novel symbionts in the deep terrestrial RT subsurface."; RL Submitted (SEP-2017) 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}. 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|HAMAP-Rule:MF_00444, CC ECO:0000256|PROSITE-ProRule:PRU10085}; 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PIU98472.1}. 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; PEVJ01000028; PIU98472.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2M7B5X6; -. DR Proteomes; UP000228949; Unassembled WGS sequence. 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; 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; PS00381; CLP_PROTEASE_SER; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00444}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00444}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00444}; KW Serine protease {ECO:0000256|HAMAP-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" SQ SEQUENCE 194 AA; 21308 MW; BA3401C03F011315 CRC64; MDFIPMVIEK NPSGERAYDI YSRLLKERII FIGGPINDAV ANSVIAQMLF LEHEDSKKDI TLYLNTPGGA VTAGLAIYDT IQYIKPDIST ICVGLAASMG AVLLAAGAKG KRFILPNSEV MLHQVMGEAG GQAVEIEITA RQILKIKDKI NELLAKHTGQ PLSRIEKDTD RDFYLSAQES KEYGLVDGII KNKR //