ID   CLPP_CHLMO              Reviewed;        1010 AA.
AC   P42379;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   22-FEB-2023, entry version 111.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
DE   Contains:
DE     RecName: Full=Ceu clpP intein;
DE     AltName: Full=Insertion IS2;
GN   Name=clpP;
OS   Chlamydomonas moewusii (Chlamydomonas eugametos).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8052234; DOI=10.1007/bf00283516;
RA   Huang C., Wang S., Chen L., Lemieux C., Otis C., Turmel M., Liu X.-Q.;
RT   "The Chlamydomonas chloroplast clpP gene contains translated large
RT   insertion sequences and is essential for cell growth.";
RL   Mol. Gen. Genet. 244:151-159(1994).
RN   [2]
RP   PROTEIN SPLICING.
RX   PubMed=9115246; DOI=10.1074/jbc.272.18.11869;
RA   Wang S., Liu X.-Q.;
RT   "Identification of an unusual intein in chloroplast ClpP protease of
RT   Chlamydomonas eugametos.";
RL   J. Biol. Chem. 272:11869-11873(1997).
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 (By similarity).
CC       {ECO:0000250}.
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|PROSITE-
CC         ProRule:PRU10085, ECO:0000255|PROSITE-ProRule:PRU10086};
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC   -!- DOMAIN: This gene contains two large insertion sequences (IS1 and Ceu
CC       clpP intein) that divide the clpP gene into three sequence domains.
CC       Each insertion sequence forms a continuous open reading frame with its
CC       upstream and downstream sequence domains.
CC   -!- PTM: This protein undergoes a protein self splicing that involves a
CC       post-translational excision of the intervening region (intein) followed
CC       by peptide ligation.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR   EMBL; L29402; AAA84150.1; -; Genomic_DNA.
DR   PIR; T09499; T09499.
DR   AlphaFoldDB; P42379; -.
DR   SMR; P42379; -.
DR   MEROPS; N11.001; -.
DR   MEROPS; S14.007; -.
DR   BRENDA; 3.4.21.92; 1316.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   CDD; cd00081; Hint; 1.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 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   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   PANTHER; PTHR10381; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10381:SF11; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF00574; CLP_protease; 2.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Chloroplast; Hydrolase; Plastid; Protease;
KW   Protein splicing; Serine protease.
FT   CHAIN           1..447
FT                   /note="ATP-dependent Clp protease proteolytic subunit, 1st
FT                   part"
FT                   /id="PRO_0000005513"
FT   CHAIN           448..903
FT                   /note="Ceu clpP intein"
FT                   /id="PRO_0000005514"
FT   CHAIN           904..1010
FT                   /note="ATP-dependent Clp protease proteolytic subunit, 2nd
FT                   part"
FT                   /id="PRO_0000005515"
FT   DOMAIN          590..728
FT                   /note="DOD-type homing endonuclease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT   REGION          60..377
FT                   /note="Insertion IS1"
FT   REGION          73..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        419
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10085,
FT                   ECO:0000255|PROSITE-ProRule:PRU10086"
FT   ACT_SITE        444
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1010 AA;  114552 MW;  886463C9F781D0A6 CRC64;
     MPIGVPRIIY CWGEELPAQW TDIYNFIFRR RMVFLMQYLD DELCNQICGL LINIHMEDRS
     KELEKKEIER SGLFKGGPKT QKGGTGAGET GASSIQNKKS NSSSFEDLLA ADEDLGIDEN
     NTLEQYTLQK ITMEWLNWNA QFFDYSDEPY LFYLAEMLSK DFNKGDARML FSNNNKFSMP
     FSQMLNTGSM SDPRRPQSTN GANWNSSEQN NSLDIYSPFR MLANFEAQDY DFKQINPSLA
     SKEEVFKLFN NTILKNGGQR NNNMSKLLTE LAQRNWENKT NSQENLYKST EKALSQRNLR
     KEYIKDRTLN NYSSDPFNTK GYVNAQGAST GPSPRTRGMH ADGSLNYLDF YSYNDSYNDF
     KTAPRGKQAE RAFQEEESKK VFVIINSFGG SVGNGITVHD ALQFIKAGSL TLALGVAASA
     ASLALAGGTI GERYVTEGCH VMIHQPECLT SDHTVLTTRG WIPIADVTLD DKVAVLDNNT
     GEMSYQNPQK VHKYDYEGPM YEVKTAGVDL FVTPNHRMYV NTTNNTTNQN YNLVEASSIF
     GKKVRYKNDA IWNKTDYQFI LPETATLTGH TNKISSTPAI QPEMNAWLTF FGLWIANGHT
     TKIAEKTAEN NQQKQRYKVI LTQVKEDVCD IIEQTLNKLG FNFIRSGKDY TIENKQLWSY
     LNPFDNGALN KYLPDWVWEL SSQQCKILLN SLCLGNCLFT KNDDTLHYFS TSERFANDVS
     RLALHAGTTS TIQLEAAPSN LYDTIIGLPV EVNTTLWRVI INQSSFYSYS TDKSSALNLS
     NNVACYVNAQ SALTLEQNSQ KINKNTLVLT KNNVKSQTMH SQRAERVDTA LLTQKELDNS
     LNHEILINKN PGTSQLECVV NPEVNNTSTN DRFVYYKGPV YCLTGPNNVF YVQRNGKAVW
     TGNSSIQGQA SDIWIDSQEI MKIRLDVAEI YSLATYRPRH KILRDLDRDF YLTATETIHY
     GLADEIASNE VMQEIIEMTS KVWDYHDTKQ QRLLESRDST TSGADTQSQN
//