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ATP-dependent Clp protease proteolytic subunit 1, mitochondrial (EC 3.4.21.92) (Endopeptidase Clp)

 CLPP1_CAEEL             Reviewed;         221 AA.
Q27539; B6VQ47; H2FLG3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
19-JAN-2010, sequence version 2.
25-APR-2018, entry version 122.
RecName: Full=ATP-dependent Clp protease proteolytic subunit 1, mitochondrial;
EC=3.4.21.92;
AltName: Full=Endopeptidase Clp;
Flags: Precursor;
Name=clpp-1; ORFNames=ZK970.2;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2]
TISSUE SPECIFICITY.
PubMed=16354718; DOI=10.1242/dev.02185;
Pauli F., Liu Y., Kim Y.A., Chen P.J., Kim S.K.;
"Chromosomal clustering and GATA transcriptional regulation of
intestine-expressed genes in C. elegans.";
Development 133:287-295(2006).
[3]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=17925224; DOI=10.1016/j.devcel.2007.07.016;
Haynes C.M., Petrova K., Benedetti C., Yang Y., Ron D.;
"ClpP mediates activation of a mitochondrial unfolded protein response
in C. elegans.";
Dev. Cell 13:467-480(2007).
-!- FUNCTION: Clp cleaves peptides in various proteins in a process
that requires ATP hydrolysis. Clp may be responsible for a fairly
general and central housekeeping function rather than for the
degradation of specific substrates. {ECO:0000269|PubMed:17925224}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
the presence of ATP and magnesium. Alpha-casein is the usual test
substrate. In the absence of ATP, only oligopeptides shorter than
five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-
Leu- and -Tyr-|-Trp bonds also occurs).
-!- SUBUNIT: Tetradecamer that assembles into a two heptameric rings
with a central cavity. {ECO:0000269|PubMed:17925224}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:17925224}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=d;
IsoId=Q27539-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=b;
IsoId=Q27539-2; Sequence=VSP_039409;
Note=No experimental confirmation available.;
Name=a;
IsoId=Q27539-3; Sequence=VSP_044103;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the intestine.
{ECO:0000269|PubMed:16354718}.
-!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z49073; CAA88886.1; -; Genomic_DNA.
EMBL; Z49073; CAR97864.1; -; Genomic_DNA.
EMBL; Z49073; CCF23347.1; -; Genomic_DNA.
PIR; C88288; C88288.
RefSeq; NP_001254239.1; NM_001267310.1. [Q27539-1]
RefSeq; NP_001254240.1; NM_001267311.1. [Q27539-3]
RefSeq; NP_001254241.1; NM_001267312.1. [Q27539-2]
UniGene; Cel.13727; -.
ProteinModelPortal; Q27539; -.
SMR; Q27539; -.
STRING; 6239.ZK970.2d; -.
MEROPS; S14.A04; -.
EPD; Q27539; -.
PaxDb; Q27539; -.
PeptideAtlas; Q27539; -.
PRIDE; Q27539; -.
EnsemblMetazoa; ZK970.2d; ZK970.2d; WBGene00014172. [Q27539-1]
GeneID; 174594; -.
KEGG; cel:CELE_ZK970.2; -.
CTD; 174594; -.
WormBase; ZK970.2a; CE02402; WBGene00014172; clpp-1. [Q27539-3]
WormBase; ZK970.2b; CE43229; WBGene00014172; clpp-1. [Q27539-2]
WormBase; ZK970.2d; CE47044; WBGene00014172; clpp-1. [Q27539-1]
eggNOG; KOG0840; Eukaryota.
eggNOG; COG0740; LUCA.
GeneTree; ENSGT00390000005830; -.
HOGENOM; HOG000285833; -.
InParanoid; Q27539; -.
KO; K01358; -.
OMA; GIFDTMQ; -.
OrthoDB; EOG091G0KCO; -.
PhylomeDB; Q27539; -.
BRENDA; 3.4.21.92; 1045.
PRO; PR:Q27539; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00014172; -.
GO; GO:0005759; C:mitochondrial matrix; IDA:WormBase.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:WormBase.
GO; GO:0034514; P:mitochondrial unfolded protein response; IMP:WormBase.
GO; GO:0006508; P:proteolysis; IDA:WormBase.
CDD; cd07017; S14_ClpP_2; 1.
HAMAP; MF_00444; ClpP; 1.
InterPro; IPR001907; ClpP.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR023562; ClpP/TepA.
InterPro; IPR033135; ClpP_His_AS.
InterPro; IPR018215; ClpP_Ser_AS.
PANTHER; PTHR10381; PTHR10381; 1.
Pfam; PF00574; CLP_protease; 1.
PRINTS; PR00127; CLPPROTEASEP.
SUPFAM; SSF52096; SSF52096; 1.
PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
PROSITE; PS00381; CLP_PROTEASE_SER; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Hydrolase; Mitochondrion;
Protease; Reference proteome; Serine protease; Transit peptide.
TRANSIT 1 25 Mitochondrion. {ECO:0000250}.
CHAIN 26 221 ATP-dependent Clp protease proteolytic
subunit 1, mitochondrial.
/FTId=PRO_0000179762.
ACT_SITE 120 120 Nucleophile. {ECO:0000305}.
ACT_SITE 145 145 {ECO:0000305}.
VAR_SEQ 1 104 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_039409.
VAR_SEQ 1 15 Missing (in isoform a). {ECO:0000305}.
/FTId=VSP_044103.
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


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