ID B0SRL7_LEPBP Unreviewed; 202 AA. AC B0SRL7; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 02-SEP-2026, entry version 108. 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=clpP1 {ECO:0000313|EMBL:ABZ97812.1}; GN Synonyms=clpP {ECO:0000256|HAMAP-Rule:MF_00444}; GN OrderedLocusNames=LEPBI_I1706 {ECO:0000313|EMBL:ABZ97812.1}; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris). OC Bacteria; Pseudomonadati; Spirochaetota; Leptospiria; Leptospirales; OC Leptospiraceae; Leptospira. OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97812.1, ECO:0000313|Proteomes:UP000001847}; RN [1] {ECO:0000313|EMBL:ABZ97812.1, ECO:0000313|Proteomes:UP000001847} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Patoc 1 / ATCC 23582 / Paris RC {ECO:0000313|Proteomes:UP000001847}; RX PubMed=18270594; DOI=10.1371/journal.pone.0001607; RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.; RT "Genome sequence of the saprophyte Leptospira biflexa provides insights RT into the evolution of Leptospira and the pathogenesis of leptospirosis."; RL PLoS ONE 3:E1607-E1607(2008). 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; CP000786; ABZ97812.1; -; Genomic_DNA. DR RefSeq; WP_012388690.1; NC_010602.1. DR AlphaFoldDB; B0SRL7; -. DR STRING; 456481.LEPBI_I1706; -. DR MEROPS; S14.005; -. DR KEGG; lbi:LEPBI_I1706; -. DR HOGENOM; CLU_058707_4_0_12; -. DR OrthoDB; 350336at2; -. DR BioCyc; LBIF456481:LEPBI_RS08430-MONOMER; -. DR Proteomes; UP000001847; Chromosome I. 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:000055; 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; NF009205; PRK12553.1; 1. DR PANTHER; PTHR10381; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1. DR PANTHER; PTHR10381:SF11; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT, MITOCHONDRIAL; 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|ARBA:ARBA00022490, 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:UP000001847}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP- KW Rule:MF_00444}. FT ACT_SITE 102 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10085" FT ACT_SITE 102 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00444" FT ACT_SITE 127 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00444, FT ECO:0000256|PROSITE-ProRule:PRU10086" SQ SEQUENCE 202 AA; 22421 MW; 6CF3EC9BEE3ED355 CRC64; MPEEETPEKE ITETIQDLIS DKNMGKKFLE KRKIFLWGPV TDESSKELTA KLMYLEMVDP GKPITFYINS PGGVVTSGLV VYDTMQMISS PVHTVCMGMA ASMGSILLIG GKKGNRYIWP NGRVMIHQPS IGGQIQAPAT DLLIHAQDIV KTKEKLNQML ADACGKSYEQ LVEDTDRDYY MDAEQALAYG IVDKIVNTID VV //