ID   CLPP_PSEP1              Reviewed;         213 AA.
AC   A5W635;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Pput_3469;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) 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; CP000712; ABQ79595.1; -; Genomic_DNA.
DR   RefSeq; WP_003259400.1; NC_009512.1.
DR   AlphaFoldDB; A5W635; -.
DR   SMR; A5W635; -.
DR   STRING; 351746.Pput_3469; -.
DR   MEROPS; S14.001; -.
DR   EnsemblBacteria; ABQ79595; ABQ79595; Pput_3469.
DR   GeneID; 58530203; -.
DR   KEGG; ppf:Pput_3469; -.
DR   eggNOG; COG0740; Bacteria.
DR   HOGENOM; CLU_058707_3_2_6; -.
DR   OMA; RDYWMKA; -.
DR   OrthoDB; 1728970at2; -.
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   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   Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..213
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_1000026115"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   213 AA;  23515 MW;  B40284CE0671B146 CRC64;
     MSRNSYIQQS SDIQAAGGLV PMVIEQSARG ERAYDIYSRL LKERVIFLVG PVEDYMANLV
     VAQLLFLEAE NPDKDIHLYI NSPGGSVTAG MSIYDTMQFI KPDVSTICIG QACSMGAFLL
     AAGAKGKRHC LPNSRVMIHQ PLGGFQGQAT DIEIHAQEIL NIKARLNELL AYHTGQDLET
     IKRDTERDNF MSASRAAEYG LIDSVYDKRQ LAS