AC   MF_00444;
DC   Protein; auto
TR   HAMAP; MF_00444; -; 1; level=0
XX
Names: ClpP
XX
ID   CLPP
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp;
GN   Name=clpP;
XX
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.
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;
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
CC   -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which
CC       stack back to back to give a disk-like structure with a central cavity,
CC       resembling the structure of eukaryotic proteasomes. Component of the
CC       ClpAP and ClpXP complexes.
else case <OC:Bacteria>
CC   -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which
CC       stack back to back to give a disk-like structure with a central cavity,
CC       resembling the structure of eukaryotic proteasomes.
else case <OC:Viridiplantae>
CC   -!- SUBUNIT: Component of the chloroplastic Clp protease core complex.
end case
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
end case
case not <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
XX
DR   Pfam; PF00574; CLP_protease; 1; trigger=no
DR   PRINTS; PR00127; CLPPROTEASEP; 1; trigger=no
DR   NCBIfam; TIGR00493; ClpP; 1; trigger=no
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1; trigger=no
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1; trigger=no
XX
case not <OG:Chloroplast>
KW   Cytoplasm
end case
KW   Hydrolase
KW   Protease
KW   Serine protease
XX
GO   GO:0004252; F:serine-type endopeptidase activity
GO   GO:0006508; P:proteolysis
case <OG:Chloroplast>
GO   GO:0009570; C:chloroplast stroma
end case
case not <OG:Chloroplast>
GO   GO:0005737; C:cytoplasm
end case
XX
FT   From: CLPP_ECOLI (P0A6G7)
FT   ACT_SITE        111
FT                   /note="Nucleophile"
FT   Condition: S
FT   ACT_SITE        136
FT   Condition: H
XX
Size: 180-249;
Related: None;
Template: P0A6G7;
Scope:
 Bacteria
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: in AGRFC, BACAN, BACC1, BACCR, BACCZ, BACHK, BACLD, SHOC1, BIFLO,
 BORBU, BRADU, PARXL, CHLAB, CHLFF, CHLMU, CHLPN, CHLTA, CHLTR, CORDI, COREF,
 CORJK, CYAPA, DESHY, GLOVI, GLUOX, LEIXX, LEPIC, CHESB, METAC, MIXXD, MYCLE,
 MYCPA, MYCTU, NOCFA, PARUW, CUTAK, PROM9, PROMA, PROMM, PROMP, PROMT, PSEAE,
 RHIEC, RHIJ3, RHILO, RHIME, RHOBA, RHOJR, SALRD, STRAW, STRCO, SYMTH, SYNJA,
 SYNJB, SYNP6, SYNE7, PARMW, SYNS9, SYNSC, SYNY3, THEFY, TREDE, TROW8, TROWT
Plasmid: None
Comments: In Bacillus subtilis and also probably in some other Bacillaceae,
 ClpXP plays a major role in the third proteolytic step of stress-induced
 degradation of anti-sigma-W factor RsiW (PubMed=16899079).
 A number of possible inactive clpP-like protein have not been shown in
 the alignment (clpP4 from STRCO, clpR from SYNY3, etc.).
 Inteins deleted in CHLEU (not shown in alignment).
 Weird insert in CHLRE (not shown in alignment).
XX
# Revision 1.54 2023/11/28
//