ID A0A1G3C1Q0_9BACT Unreviewed; 197 AA. AC A0A1G3C1Q0; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 27-NOV-2024, entry version 29. 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; Planctomycetota. OX NCBI_TaxID=1801983 {ECO:0000313|EMBL:OHC01407.1, ECO:0000313|Proteomes:UP000177189}; RN [1] {ECO:0000313|EMBL:OHC01407.1, ECO:0000313|Proteomes:UP000177189} 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., Brodie E.L., RA Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected biogeochemical RT 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 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 -!- 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: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 AlphaFoldDB; A0A1G3C1Q0; -. DR Proteomes; UP000177189; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009368; C:endopeptidase Clp complex; IEA:TreeGrafter. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR GO; GO:0051117; F:ATPase binding; IEA:TreeGrafter. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:TreeGrafter. 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; 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. 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 Membrane {ECO:0000256|SAM:Phobius}; 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}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 88..107 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" 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 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 //