ID A9GIS3_SORC5 Unreviewed; 214 AA. AC A9GIS3; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 04-NOV-2026, entry version 104. 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 Synonyms=clpP2 {ECO:0000313|EMBL:CAN93306.1}; GN OrderedLocusNames=sce3147 {ECO:0000313|EMBL:CAN93306.1}; OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So OS ce56)). OC Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales; OC Polyangiaceae; Sorangium. OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN93306.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN93306.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; RX PubMed=17965706; DOI=10.1038/nbt1354; RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O., RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J., RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A., RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C., RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T., RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S., RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G., RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., RA Puehler A., Mueller R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). 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; AM746676; CAN93306.1; -; Genomic_DNA. DR RefSeq; WP_012235778.1; NC_010162.1. DR AlphaFoldDB; A9GIS3; -. DR STRING; 448385.sce3147; -. DR MEROPS; S14.001; -. DR KEGG; scl:sce3147; -. DR eggNOG; COG0740; Bacteria. DR HOGENOM; CLU_058707_3_2_7; -. DR OrthoDB; 9802800at2; -. DR BioCyc; SCEL448385:SCE_RS16125-MONOMER; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009368; C:endopeptidase Clp complex; IEA:TreeGrafter. 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule. DR CDD; cd07017; S14_ClpP_2; 1. DR FunFam; 3.90.226.10:FF:000001; ATP-dependent Clp protease proteolytic subunit; 1. DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 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; NF001368; PRK00277.1; 1. DR NCBIfam; NF009205; PRK12553.1; 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 Reference proteome {ECO:0000313|Proteomes:UP000002139}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP- KW Rule:MF_00444}. FT ACT_SITE 117 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10085" FT ACT_SITE 117 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00444" FT ACT_SITE 142 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00444, FT ECO:0000256|PROSITE-ProRule:PRU10086" SQ SEQUENCE 214 AA; 24211 MW; 0BC83C4CAFBF777C CRC64; MTRRVETRTQ AIEFLEREKA YILPTVTEVT HRGEREWNIF SRLLKDRIVF IGTEIDDFVA NAVIAQFLFL ESEDPEKEIQ VYINSPGGVV TSGLAMYDTM QYVRCPVSTM CIGQAASMGA VLLGAGRKGR RFALPHARMM IHQPLGGARG QATDIEIQAR EIKKIKETLI DILVDATGKN RDELAKDIER DFYLSATQAK EYGLIDEVFP KRNK //