CLPPL_CYAPA
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 03-AUG-2022, entry version 75.
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; Cyanophoraceae; Cyanophora.
OX NCBI_TaxID=2762;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
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;
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}.
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DR EMBL; U30821; AAA81214.1; -; Genomic_DNA.
DR PIR; T06871; T06871.
DR RefSeq; NP_043183.1; NC_001675.1.
DR AlphaFoldDB; P48254; -.
DR SMR; P48254; -.
DR GeneID; 801552; -.
DR GO; GO:0009842; C:cyanelle; IEA:UniProtKB-SubCell.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07017; S14_ClpP_2; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 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