ID   CLPP1_CAEBR             Reviewed;         219 AA.
AC   A8WPG6;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit 1, mitochondrial {ECO:0000250|UniProtKB:Q27539};
DE            EC=3.4.21.92;
DE   Flags: Precursor;
GN   Name=clpp-1 {ECO:0000312|EMBL:CAP22373.2}; ORFNames=CBG00853;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP22373.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Clp cleaves peptides in various proteins in a process that
CC       requires ATP hydrolysis. Clp may be responsible for a fairly general
CC       and central housekeeping function rather than for the degradation of
CC       specific substrates (By similarity). {ECO:0000250|UniProtKB:Q27539}.
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};
CC   -!- SUBUNIT: Tetradecamer that assembles into a two heptameric rings with a
CC       central cavity. {ECO:0000250|UniProtKB:Q27539}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q27539}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255}.
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DR   EMBL; HE600951; CAP22373.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8WPG6; -.
DR   SMR; A8WPG6; -.
DR   STRING; 6238.CBG00853; -.
DR   MEROPS; S14.A04; -.
DR   PRIDE; A8WPG6; -.
DR   EnsemblMetazoa; CBG00853.1; CBG00853.1; WBGene00024182.
DR   WormBase; CBG00853; CBP30799; WBGene00024182; Cbr-clpp-1.
DR   eggNOG; KOG0840; Eukaryota.
DR   HOGENOM; CLU_058707_3_0_1; -.
DR   InParanoid; A8WPG6; -.
DR   OMA; RDYWMKA; -.
DR   OrthoDB; 1274502at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0034514; P:mitochondrial unfolded protein response; IEA:EnsemblMetazoa.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Mitochondrion; Protease; Reference proteome; Serine protease;
KW   Transit peptide.
FT   TRANSIT         1..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q27539"
FT   CHAIN           24..219
FT                   /note="ATP-dependent Clp protease proteolytic subunit 1,
FT                   mitochondrial"
FT                   /evidence="ECO:0000250|UniProtKB:Q27539"
FT                   /id="PRO_0000395329"
FT   ACT_SITE        118
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   219 AA;  24150 MW;  B578E80EDE9E669B CRC64;
     MLRRILTTSS VRNLTSSTQA RVGIPFVIDN EGKGERTYDI YSRLLRDRIV CLMTPVDDFM
     ASALIAQLLF LQSESSKKPI HMYINSPGGS VTAGLAIYDT MQMISAPVAT WVIGQASSMG
     SLLLAAGEKG MRSALPNARI MVHQPSGGAQ GTCSDIVIRA EEITRLKKRL NEIYVHHTGI
     SYDEIERTLD RDRFMSAQEA LKFGLVDKIE KHTGSMPTD