CLPP_BOVIN
ID CLPP_BOVIN Reviewed; 272 AA.
AC Q2KHU4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit, mitochondrial;
DE EC=3.4.21.92 {ECO:0000250|UniProtKB:Q16740};
DE AltName: Full=Endopeptidase Clp;
DE Flags: Precursor;
GN Name=CLPP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protease component of the Clp complex that cleaves peptides
CC and various proteins in an ATP-dependent process. Has low peptidase
CC activity in the absence of CLPX. The Clp complex can degrade CSN1S1,
CC CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be
CC responsible for a fairly general and central housekeeping function
CC rather than for the degradation of specific substrates. Cleaves PINK1
CC in the mitochondrion. {ECO:0000250|UniProtKB:Q16740}.
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:0000250|UniProtKB:Q16740};
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 Component of the Clp complex formed by the assembly of two CLPP
CC heptameric rings with two CLPX hexameric rings, giving rise to a
CC symmetrical structure with two central CLPP rings flanked by a CLPX
CC ring at either end of the complex. {ECO:0000250|UniProtKB:Q16740}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q16740}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR EMBL; BC112880; AAI12881.1; -; mRNA.
DR RefSeq; NP_001039879.1; NM_001046414.2.
DR AlphaFoldDB; Q2KHU4; -.
DR SMR; Q2KHU4; -.
DR STRING; 9913.ENSBTAP00000019577; -.
DR MEROPS; S14.003; -.
DR PaxDb; Q2KHU4; -.
DR PeptideAtlas; Q2KHU4; -.
DR PRIDE; Q2KHU4; -.
DR Ensembl; ENSBTAT00000019577; ENSBTAP00000019577; ENSBTAG00000014712.
DR GeneID; 535981; -.
DR KEGG; bta:535981; -.
DR CTD; 8192; -.
DR VEuPathDB; HostDB:ENSBTAG00000014712; -.
DR VGNC; VGNC:27459; CLPP.
DR eggNOG; KOG0840; Eukaryota.
DR GeneTree; ENSGT00390000005830; -.
DR HOGENOM; CLU_058707_3_0_1; -.
DR InParanoid; Q2KHU4; -.
DR OMA; RDYWMKA; -.
DR OrthoDB; 1274502at2759; -.
DR TreeFam; TF105002; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014712; Expressed in laryngeal cartilage and 104 other tissues.
DR GO; GO:0009368; C:endopeptidase Clp complex; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; IEA:Ensembl.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Hydrolase; Mitochondrion; Protease; Reference proteome;
KW Serine protease; Transit peptide.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..272
FT /note="ATP-dependent Clp protease proteolytic subunit,
FT mitochondrial"
FT /id="PRO_0000260318"
FT REGION 240..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 174
FT /evidence="ECO:0000250"
FT MOD_RES 196
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88696"
FT MOD_RES 207
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16740"
SQ SEQUENCE 272 AA; 29704 MW; 093E2BF04EA98EDC CRC64;
MWPKILLRGG RVAAGLCPAL GPRLAARFPP QRTPENRLAP QRNLHATAAR ALPLIPIVVE
QTGRGERAYD IYSRLLRERI VCVMGPIDDS VASLVIAQLL FLQSESNKKP IHMYINSPGG
VVTSGLAIYD TMQYILNPIC TWCVGQAASM GSLLLAAGTP GMRHSLPNSR IMIHQPSGGA
RGQATDIAIQ AEEIMKLKKQ LYSIYAKHTK QSLQVIESAM ERDRYMSPME AQEFGILDKV
LVHPPQDGED EPELVQKEPG EPTAVEPAPA SA
