ID   CLPP_BORPA              Reviewed;         217 AA.
AC   Q7W8X2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=BPP2006;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640429; CAE37306.1; -; Genomic_DNA.
DR   RefSeq; WP_003812508.1; NC_002928.3.
DR   AlphaFoldDB; Q7W8X2; -.
DR   SMR; Q7W8X2; -.
DR   MEROPS; S14.001; -.
DR   EnsemblBacteria; CAE37306; CAE37306; BPP2006.
DR   GeneID; 56478369; -.
DR   GeneID; 66438505; -.
DR   KEGG; bpa:BPP2006; -.
DR   HOGENOM; CLU_058707_3_2_4; -.
DR   OMA; RDYWMKA; -.
DR   Proteomes; UP000001421; 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   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; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..217
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000179512"
FT   ACT_SITE        119
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ   SEQUENCE   217 AA;  23775 MW;  E2F2B2D264FDF6E1 CRC64;
     MQRFTDFYAA MHGGSSVTPT GLGYIPMVIE QSGRGERAYD IYSRLLRERL IFLVGPVNDN
     TANLVVAQLL FLESENPDKD ISFYINSPGG SVYAGMAIYD TMQFIKPDVS TLCTGLAASM
     GAFLLAAGKK GKRFTLPNSR IMIHQPSGGA QGQASDIQIQ AREILDLRER LNRILAENTG
     QPVERIAVDT ERDNFMSAED AVSYGLVDKV LTSRAQT