ID I0BRS6_9BACL Unreviewed; 196 AA. AC I0BRS6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-SEP-2017, entry version 36. 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 ORFNames=B2K_30945 {ECO:0000313|EMBL:AFH65073.1}; OS Paenibacillus mucilaginosus K02. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH65073.1, ECO:0000313|Proteomes:UP000007392}; RN [1] {ECO:0000313|EMBL:AFH65073.1, ECO:0000313|Proteomes:UP000007392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K02 {ECO:0000313|EMBL:AFH65073.1, RC ECO:0000313|Proteomes:UP000007392}; RA Xiao B., Sun L., Xiao L., Lian B.; RT "Complete genome sequence of Paenibacillus mucilaginosus K02."; RL Submitted (JUN-2013) 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, ECO:0000256|RuleBase:RU000550, CC ECO:0000256|SAAS:SAAS00674840}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in CC the presence of ATP and magnesium. Alpha-casein is the usual test CC substrate. In the absence of ATP, only oligopeptides shorter than CC five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; CC and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|- CC Leu- and -Tyr-|-Trp bonds also occurs). {ECO:0000256|HAMAP- CC Rule:MF_00444, ECO:0000256|PROSITE-ProRule:PRU10085, CC ECO:0000256|RuleBase:RU000549, ECO:0000256|SAAS:SAAS00674888}. 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 ECO:0000256|SAAS:SAAS00674837}. 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; CP003422; AFH65073.1; -; Genomic_DNA. DR RefSeq; WP_013920148.1; NC_017672.3. DR MEROPS; S14.001; -. DR EnsemblBacteria; AFH65073; AFH65073; B2K_30945. DR KEGG; pmw:B2K_30945; -. DR PATRIC; fig|997761.3.peg.6195; -. DR KO; K01358; -. DR OrthoDB; POG091H01WN; -. DR Proteomes; UP000007392; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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. DR InterPro; IPR023562; ClpP/TepA. DR InterPro; IPR033135; ClpP_His_AS. DR InterPro; IPR018215; ClpP_Ser_AS. DR PANTHER; PTHR10381; PTHR10381; 1. DR Pfam; PF00574; CLP_protease; 1. DR PRINTS; PR00127; CLPPROTEASEP. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR00493; clpP; 1. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007392}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00444, KW ECO:0000256|RuleBase:RU000549, ECO:0000256|SAAS:SAAS00674918}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00444, KW ECO:0000256|RuleBase:RU000549, ECO:0000256|SAAS:SAAS00674844, KW ECO:0000313|EMBL:AFH65073.1}; KW Serine protease {ECO:0000256|HAMAP-Rule:MF_00444, KW ECO:0000256|RuleBase:RU000549, ECO:0000256|SAAS:SAAS00674861}. FT ACT_SITE 98 98 {ECO:0000256|PROSITE-ProRule:PRU10085}. 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 196 AA; 21462 MW; 9AFA59087989C59A CRC64; MTLVPMVVEQ EGRGERSYDI YSRLLKDRII FLGSAIDDDV ANLVIAQLLF LAATDPDKDI HLYINSPGGS VTAGMGIYDT MQFIKPDVST ICVGLAASMG SLLLTAGAPG KRFALPNSEV MIHQPLGGVR GQASDIKIHA DWIIKTKRKL NEIYVARTGQ PYDKIERDTD RDNFMSAAEA KEYGLIDAVI TRSDLT //