ID A0A1G3C1Q0_9BACT Unreviewed; 197 AA. AC A0A1G3C1Q0; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 05-DEC-2018, entry version 16. 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 ORFNames=A3H23_07060 {ECO:0000313|EMBL:OHC01407.1}; OS Planctomycetes bacterium RIFCSPLOWO2_12_FULL_40_19. OC Bacteria; Planctomycetes. OX NCBI_TaxID=1801983 {ECO:0000313|EMBL:OHC01407.1}; RN [1] {ECO:0000313|EMBL:OHC01407.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27774985; DOI=10.1038/ncomms13219; RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J., RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., RA Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected RT biogeochemical processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). 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 CC of ATP and magnesium. Alpha-casein is the usual test substrate. CC In the absence of ATP, only oligopeptides shorter than five CC residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and CC Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and CC -Tyr-|-Trp bonds also occurs).; EC=3.4.21.92; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|PROSITE- CC ProRule:PRU10086}; CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings CC which stack back to back to give a disk-like structure with a CC central cavity, resembling the structure of eukaryotic CC proteasomes. {ECO:0000256|HAMAP-Rule:MF_00444}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OHC01407.1}. 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; MHZA01000163; OHC01407.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; 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 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. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00444}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00444, KW ECO:0000313|EMBL:OHC01407.1}; KW Serine protease {ECO:0000256|HAMAP-Rule:MF_00444}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 88 107 Helical. {ECO:0000256|SAM:Phobius}. FT ACT_SITE 98 98 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_00444}. FT ACT_SITE 123 123 {ECO:0000256|HAMAP-Rule:MF_00444, FT ECO:0000256|PROSITE-ProRule:PRU10086}. SQ SEQUENCE 197 AA; 22190 MW; A19BB54D8CBB5B49 CRC64; MKEINFKDDV EKDNQRLDLI GAKLMKNRTI MITDVITKRL AQRTIAQLLI MEQEYPEKEI KVFINSPGGD ADAGFAIYDM MKFVKPRIIN ICAGVAASAA VIILLGTGRE NRISLPNARI LIHQPSTGVH GTASDIQIEA SEILKCREKI NRMIAEETNQ AFEKVENDTK RNYWMSAEEA VKYGLISKII KTHSDLL //