ID   CLPP_ACISJ              Reviewed;         202 AA.
AC   A1W5B6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
DE            EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE   AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
GN   Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=Ajs_1209;
OS   Acidovorax sp. (strain JS42).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX   NCBI_TaxID=232721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS42;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL   Submitted (DEC-2006) 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:0000255|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:0000255|HAMAP-Rule:MF_00444};
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:0000255|HAMAP-
CC       Rule:MF_00444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
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DR   EMBL; CP000539; ABM41441.1; -; Genomic_DNA.
DR   RefSeq; WP_011804641.1; NC_008782.1.
DR   AlphaFoldDB; A1W5B6; -.
DR   SMR; A1W5B6; -.
DR   STRING; 232721.Ajs_1209; -.
DR   MEROPS; S14.001; -.
DR   EnsemblBacteria; ABM41441; ABM41441; Ajs_1209.
DR   KEGG; ajs:Ajs_1209; -.
DR   eggNOG; COG0740; Bacteria.
DR   HOGENOM; CLU_058707_3_2_4; -.
DR   OMA; RDYWMKA; -.
DR   Proteomes; UP000000645; Chromosome.
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   GO; GO:0006508; P:proteolysis; 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   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00493; clpP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..202
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_1000026060"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   202 AA;  22271 MW;  6176159CA77C030C CRC64;
     MSALETQALG MIPMVIEQSG RGERSYDIYS RLLKERVIFL VGEVNDQTAN LVVAQLLFLE
     SENPDKDISF YINSPGGSVT AGMAIYDTMQ FIKPDVSTLC CGFAASMGAF LLAAGAKGKR
     YSLPNSKIMI HQVLGGARGQ ATDIEIHARD ILRTKEQMNR ILAERTGQPI EKVKADTERD
     YFMTADEAKD YGIVDQVIAK RP