ID A0A553XZZ2_9GAMM Unreviewed; 225 AA. AC A0A553XZZ2; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 19-JAN-2022, entry version 7. 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 ECO:0000313|EMBL:TSB22496.1}; GN ORFNames=FOR85_09880 {ECO:0000313|EMBL:TSB22496.1}; OS Psychrobacter sp. YGAH215. OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Psychrobacter. OX NCBI_TaxID=2596826 {ECO:0000313|EMBL:TSB22496.1, ECO:0000313|Proteomes:UP000317041}; RN [1] {ECO:0000313|EMBL:TSB22496.1, ECO:0000313|Proteomes:UP000317041} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YGAH215 {ECO:0000313|EMBL:TSB22496.1, RC ECO:0000313|Proteomes:UP000317041}; RA Lv Q., Li S.; RT "Draft genome sequencing of Psychrobacter sp. YGAH215."; RL Submitted (JUL-2019) 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}. 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:ARBA00001048, 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:TSB22496.1}. 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; VKLR01000022; TSB22496.1; -; Genomic_DNA. DR Proteomes; UP000317041; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. 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 TIGRFAMs; TIGR00493; clpP; 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 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}. FT ACT_SITE 126 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00444" FT ACT_SITE 151 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00444, FT ECO:0000256|PROSITE-ProRule:PRU10086" SQ SEQUENCE 225 AA; 25087 MW; 9A8CD865FBC73FAA CRC64; MTDYDRIIAN PHFDMLMSAH DNVQSTTQAA LVPMVVEQSA RGERSFDIFS RLLRERVIFL TGQVEDHMAN LIVAQLLFLE AENPDKDIHL YINSPGGSVS AGLAIFDTMN FIKPEVSTIC MGGAYSMGSF LLAAGEKGKR YALANSRVMI HQPSGGAQGQ ATDIEINARE ILKTRARLNE ILAERTGQPV EKIEKDVERD YWLDAKEAKE YGLVDEVLER RPDSL //