[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CWL029; DOI=10.1038/7716; PubMed=10192388 [NCBI, ExPASy, EBI, Israel, Japan] Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.; "Comparative genomes of Chlamydia pneumoniae and C. trachomatis."; Nat. Genet. 21:385-389(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=AR39; DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan] Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.; "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."; Nucleic Acids Res. 28:1397-1406(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=J138; DOI=10.1093/nar/28.12.2311; PubMed=10871362 [NCBI, ExPASy, EBI, Israel, Japan] Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.; "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."; Nucleic Acids Res. 28:2311-2314(2000).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=TW-183; Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.; "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.

Comments

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).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the peptidase S14 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE001363; AAD18660.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE002161; AAF38099.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000008; BAA98726.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017158; AAP98470.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D86555; D86555.
G72067; G72067.

RefSeq

NP_224716.1; -.
NP_300575.1; -.
NP_444784.1; -.
NP_876813.1; -.

3D structure databases

HSSP

P19245; 1TYF. [HSSP ENTRY / PDB]

ModBase

Q9Z832.

Protein family/group databases

MEROPS

S14.005; -.

Enzyme and pathway databases

BioCyc

CPNE115711:CP_0233-MON; -.
CPNE115713:CPN0520-MON; -.
CPNE138677:CPJ0520-MON; -.
CPNE182082:CPB0541-MON; -.

2D gel databases

PHCI-2DPAGE

Q9Z832; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from HAMAP).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00444; -; 1.
PBIL [Tree]

InterPro

IPR001907; Pept_S14_ClpP.
Graphical view of domain structure.

PANTHER

PTHR10381; Pept_S14_ClpP; 1.

Pfam

PF00574; CLP_protease; 1.
Pfam graphical view of domain structure.

PRINTS

PR00127; CLPPROTEASEP.

PROSITE

PS00382; CLP_PROTEASE_HIS; 1.
PS00381; CLP_PROTEASE_SER; FALSE_NEG.

ProtoNet

Q9Z832.

Genome annotation databases

GeneID

1467220; -.
895481; -.
919275; -.
962928; -.

GenomeReviews

BA000008_GR; clpP1.
AE002161_GR; CP_0233.
AE009440_GR; CpB0541.
AE001363_GR; CPn_0520.

KEGG

cpa:CP0233; -.
cpn:CPn0520; -.
cpt:CpB0541; -.

TIGR

CP_0233; -.

Phylogenomic databases

HOGENOM

Q9Z832; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Hydrolase; Protease; Serine protease.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 191`	`191`	`ATP-dependent Clp protease proteolytic subunit 1.`	`PRO_0000179532`
`ACT_SITE`	`91 91`		`By similarity.`
`ACT_SITE`	`116 116`		`By similarity.`

Sequence information

Length: 191 AA [This is the length of the unprocessed precursor]

Molecular weight: 21020 Da [This is the MW of the unprocessed precursor]

CRC64: 56F801EF1469C037 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADGEVHKLR DIIEKELLEA RRVFFSEPVT EKSASDAIKK LWYLELKDPG KPIVFVINSP 

        70         80         90        100        110        120 
GGSVDAGFAV WDQIKMLTSP VTTVVTGLAA SMGSVLSLCA APGRRFATPH SRIMIHQPSI 

       130        140        150        160        170        180 
GGPITGQATD LDIHAREILK TKARIIDVYV EATNQPRDII EKAIDRDMWM TANEAKDFGL 

       190 
LDGILFSFND L

Q9Z832 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools