CLPP1_CAEEL
ID CLPP1_CAEEL Reviewed; 221 AA.
AC Q27539; B6VQ47; H2FLG3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 1, mitochondrial;
DE EC=3.4.21.92;
DE AltName: Full=Endopeptidase Clp;
DE Flags: Precursor;
GN Name=clpp-1; ORFNames=ZK970.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16354718; DOI=10.1242/dev.02185;
RA Pauli F., Liu Y., Kim Y.A., Chen P.J., Kim S.K.;
RT "Chromosomal clustering and GATA transcriptional regulation of intestine-
RT expressed genes in C. elegans.";
RL Development 133:287-295(2006).
RN [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17925224; DOI=10.1016/j.devcel.2007.07.016;
RA Haynes C.M., Petrova K., Benedetti C., Yang Y., Ron D.;
RT "ClpP mediates activation of a mitochondrial unfolded protein response in
RT C. elegans.";
RL Dev. Cell 13:467-480(2007).
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. {ECO:0000269|PubMed:17925224}.
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;
CC -!- SUBUNIT: Tetradecamer that assembles into a two heptameric rings with a
CC central cavity. {ECO:0000269|PubMed:17925224}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:17925224}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=d;
CC IsoId=Q27539-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q27539-2; Sequence=VSP_039409;
CC Name=a;
CC IsoId=Q27539-3; Sequence=VSP_044103;
CC -!- TISSUE SPECIFICITY: Expressed in the intestine.
CC {ECO:0000269|PubMed:16354718}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR EMBL; Z49073; CAA88886.1; -; Genomic_DNA.
DR EMBL; Z49073; CAR97864.1; -; Genomic_DNA.
DR EMBL; Z49073; CCF23347.1; -; Genomic_DNA.
DR PIR; C88288; C88288.
DR RefSeq; NP_001254239.1; NM_001267310.1. [Q27539-1]
DR RefSeq; NP_001254240.1; NM_001267311.1. [Q27539-3]
DR RefSeq; NP_001254241.1; NM_001267312.1. [Q27539-2]
DR AlphaFoldDB; Q27539; -.
DR SMR; Q27539; -.
DR BioGRID; 39913; 4.
DR STRING; 6239.ZK970.2d; -.
DR MEROPS; S14.A04; -.
DR EPD; Q27539; -.
DR PaxDb; Q27539; -.
DR PeptideAtlas; Q27539; -.
DR EnsemblMetazoa; ZK970.2a.1; ZK970.2a.1; WBGene00014172. [Q27539-3]
DR EnsemblMetazoa; ZK970.2b.1; ZK970.2b.1; WBGene00014172. [Q27539-2]
DR EnsemblMetazoa; ZK970.2d.1; ZK970.2d.1; WBGene00014172. [Q27539-1]
DR GeneID; 174594; -.
DR KEGG; cel:CELE_ZK970.2; -.
DR CTD; 174594; -.
DR WormBase; ZK970.2a; CE02402; WBGene00014172; clpp-1. [Q27539-3]
DR WormBase; ZK970.2b; CE43229; WBGene00014172; clpp-1. [Q27539-2]
DR WormBase; ZK970.2d; CE47044; WBGene00014172; clpp-1. [Q27539-1]
DR eggNOG; KOG0840; Eukaryota.
DR GeneTree; ENSGT00390000005830; -.
DR InParanoid; Q27539; -.
DR OMA; GFKRQDP; -.
DR OrthoDB; 1274502at2759; -.
DR PhylomeDB; Q27539; -.
DR BRENDA; 3.4.21.92; 1045.
DR PRO; PR:Q27539; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00014172; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:WormBase.
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; IDA:WormBase.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IMP:WormBase.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:WormBase.
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 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Mitochondrion; Protease;
KW Reference proteome; Serine protease; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..221
FT /note="ATP-dependent Clp protease proteolytic subunit 1,
FT mitochondrial"
FT /id="PRO_0000179762"
FT ACT_SITE 120
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 145
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_039409"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_044103"
SQ SEQUENCE 221 AA; 24266 MW; E989F10AB1FCB139 CRC64;
MLRRLVTSSL SASRSMSASV QSRVGIPFVI DNEGKGERTY DIYSRLLRDR IVCLMTPVDD
FIASALIAQL LFLQSESGKK PIHMYINSPG GSVTAGLAIY DTIQMISAPV STWVIGQASS
MGSLLLCAGE KGMRSALPNS RIMVHQPSGG AQGTCSDIVI RAEEITRLKR RLNEIYVHHT
GMSYDEIEKT LDRDRFMSAH EALKFGLVDQ IETHNGSMPS D
