ID   B1JTV0_BURO0            Unreviewed;       217 AA.
AC   B1JTV0;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
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   OrderedLocusNames=Bcenmc03_1946 {ECO:0000313|EMBL:ACA91107.1};
OS   Burkholderia orbicola (strain MC0-3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex;
OC   Burkholderia orbicola.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA91107.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3.";
RL   Submitted (FEB-2008) 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   -!- 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}.
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DR   EMBL; CP000958; ACA91107.1; -; Genomic_DNA.
DR   RefSeq; WP_006496351.1; NC_010508.1.
DR   AlphaFoldDB; B1JTV0; -.
DR   SMR; B1JTV0; -.
DR   MEROPS; S14.001; -.
DR   GeneID; 83048721; -.
DR   KEGG; bcm:Bcenmc03_1946; -.
DR   HOGENOM; CLU_058707_3_2_4; -.
DR   Proteomes; UP000002169; Chromosome 1.
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   NCBIfam; TIGR00493; clpP; 1.
DR   PANTHER; PTHR10381; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10381:SF70; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 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|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        121
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10085"
FT   ACT_SITE        121
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00444"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00444,
FT                   ECO:0000256|PROSITE-ProRule:PRU10086"
SQ   SEQUENCE   217 AA;  23750 MW;  924F3B6062C85117 CRC64;
     MITRAELLDM LASNAPQGFE AQALGLVPIV VETSGRGERS YDIYSRLLKE RLVFMVGEVN
     DQTANLVVAQ LLFLESENPD KDISLYINSP GGSVSAGMAI YDTMQFIKPD VSTLCMGLAA
     SMGAFLLASG AKGKRFALPN SRVMIHQPLG GARGQASDIE IQAREILYLK ERLNNLLAQH
     TGQDVERIAR DTDRDNFMSS EDAKAYGLID QVLLKRP
//