ID   CLPPL_CYAPA             Reviewed;         199 AA.
AC   P48254;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 83.
DE   RecName: Full=Putative ATP-dependent Clp protease proteolytic subunit-like;
DE   AltName: Full=Endopeptidase Clp-like;
GN   Name=clpP-B; Synonyms=clpP2;
OS   Cyanophora paradoxa.
OG   Plastid; Cyanelle.
OC   Eukaryota; Glaucocystophyceae; Cyanophorales; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RX   DOI=10.1007/BF02669186;
RA   Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA   Bryant D.A.;
RT   "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL   Plant Mol. Biol. Rep. 13:327-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RX   DOI=10.1007/978-3-642-60885-8_3;
RA   Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA   Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA   Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT   "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT   genetic complexity of a primitive plastid.";
RL   (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL   (eds.);
RL   Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
CC   -!- FUNCTION: Has lost the two conserved residues (Ser and His) proposed to
CC       be part of the active site. Therefore it could be inactive.
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
CC   -!- SUBCELLULAR LOCATION: Plastid, cyanelle.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U30821; AAA81214.1; -; Genomic_DNA.
DR   PIR; T06871; T06871.
DR   AlphaFoldDB; P48254; -.
DR   SMR; P48254; -.
DR   GO; GO:0009842; C:cyanelle; IEA:UniProtKB-SubCell.
DR   GO; GO:0009368; C:endopeptidase Clp complex; IEA:TreeGrafter.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; IEA:TreeGrafter.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:TreeGrafter.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd07017; S14_ClpP_2; 1.
DR   Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 1.
DR   InterPro; IPR001907; ClpP.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR023562; ClpP/TepA.
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; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
PE   3: Inferred from homology;
KW   Cyanelle; Plastid.
FT   CHAIN           1..199
FT                   /note="Putative ATP-dependent Clp protease proteolytic
FT                   subunit-like"
FT                   /id="PRO_0000179729"
SQ   SEQUENCE   199 AA;  22195 MW;  A9F15821FB15B948 CRC64;
     MPIGYPLVKA MDKDRFISYF LINNALLNER VIFLCNYEDA TDESIYIGML LYLESENSQK
     PVSFYINSSI TFPNLCFGLY DTILQIKADI VTICLGLAGG MSSLILAAGT KGQRFALPNS
     RIMMQEPLID GGVNGQATDL AIEAKELMDT KEILINLYHE RTGQPKPVIE KDLQRPRYFS
     AQAAKEYGFI DSLLMASNG
//