HAMAP

Accession	MF_00444
Dates	1-JUN-2001 (Created) 7-OCT-2011 (Last updated, Version 37)

Data class

Protein

Predictors

HAMAP; MF_00444; [distribution of match scores in UniProtKB];[seed alignment for MF_00444]

Names

ClpP

Identifier

CLPP

Protein name

RecName: Full=ATP-dependent Clp protease proteolytic subunit; EC=3.4.21.92; AltName: Full=Endopeptidase Clp;

Gene name

clpP

FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).

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: Component of the chloroplastic Clp protease core complex (By similarity).

SUBCELLULAR LOCATION: Plastid, chloroplast stroma (By similarity).

SUBCELLULAR LOCATION: Cytoplasm (By similarity).

SIMILARITY: Belongs to the peptidase S14 family.

Pfam	PF00574; CLP_protease; 1;
PRINTS	PR00127; CLPPROTEASEP; 1;
TIGRFAMs	TIGR00493; ClpP; 1;
PROSITE	PS00381; CLP_PROTEASE_SER; 1; PS00382; CLP_PROTEASE_HIS; 1;

ATP-binding.

Cytoplasm.

Hydrolase, Nucleotide-binding, Protease, Serine protease.

GO:0004252; Molecular function: serine-type endopeptidase activity.
GO:0006508; Biological process: proteolysis.

GO:0009570; Cellular component: chloroplast stroma.

GO:0005737; Cellular component: cytoplasm.

From: CLPP_ECOLI (P0A6G7)
Key		From		To		Description		Condition		FTGroup
ACT_SITE		111		111		By similarity		S
ACT_SITE		136		136		By similarity		H

Size range:	180-249 amino acids
Related UniRules:	None
Template:	P0A6G7 (CLPP_ECOLI)
Scope:	Bacteria Plastid
Fusion:	Nter: None; Cter: None
Duplicate:	in AGRT5, BACAN, BACC1, BACCR, BACCZ, BACHK, BACLD, BACSK, BIFLO, BORBU, BRAJA, BURXL, CHLAB, CHLFF, CHLMU, CHLPN, CHLTA, CHLTR, CORDI, COREF, CORJK, CYAPA, DESHY, GLOVI, GLUOX, LEIXX, LEPIC, MESSB, METAC, MIXXD, MYCLE, MYCPA, MYCTU, NOCFA, PARUW, PROAC, PROM9, PROMA, PROMM, PROMP, PROMT, PSEAE, RHIEC, RHIL3, RHILO, RHIME, RHOBA, RHOSR, SALRD, STRAW, STRCO, SYMTH, SYNJA, SYNJB, SYNP6, SYNE7, SYNPX, SYNS9, SYNSC, SYNY3, THEFY, TREDE, TROW8, TROWT
Plasmid encoded:	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). Possible wrong starts.