Reviewed, UniProtKB/Swiss-Prot Q9Z832 (CLPP1_CHLPN)

Names and origin

Protein names

Recommended name:
    ATP-dependent Clp protease proteolytic subunit 1
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase Clp 1

Gene names

Name:	clpP1
Synonyms:	clp
Ordered Locus Names:	CPn_0520, CP_0233, CpB0541

Organism

Chlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]

Taxonomic identifier

83558 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydophila

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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). HAMAP MF_00444
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase S14 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Protease Serine protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 191	191	ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444		PRO_0000179532
Sites
	Active site	91	1	By similarity
	Active site	116	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Z832-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 56F801EF1469C037	FASTA	191	21,020
	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

References

[1]	"Comparative genomes of Chlamydia pneumoniae and C. trachomatis." 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. Nat. Genet. 21:385-389(1999) [PubMed: 10192388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CWL029.
[2]	"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." 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. Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AR39.
[3]	"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA." Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T. Nucleic Acids Res. 28:2311-2314(2000) [PubMed: 10871362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J138.
[4]	"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis." Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TW-183.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE001363 Genomic DNA. Translation: AAD18660.1. AE002161 Genomic DNA. Translation: AAF38099.1. BA000008 Genomic DNA. Translation: BAA98726.1. AE009440 Genomic DNA. Translation: AAP98470.1.
PIR	D86555. G72067.
RefSeq	NP_224716.1. NP_300575.1. NP_444784.1. NP_876813.1.
3D structure databases
HSSP	HSSP built from PDB template 1TYF based on UniProtKB P19245.
ModBase	Search...
Protein family/group databases
MEROPS	S14.005.
2-D gel databases
PHCI-2DPAGE	Q9Z832.
Genome annotation databases
GeneID	1467220. 895481. 919275. 962928.
GenomeReviews	Gene locus CPn_0520 in contig AE001363_GR. Gene locus CP_0233 in contig AE002161_GR. Gene locus CpB0541 in contig AE009440_GR. Gene locus clpP1 in contig BA000008_GR.
KEGG	cpa:CP0233. cpn:CPn0520. cpt:CpB0541.
TIGR	CP_0233.
Phylogenomic databases
HOGENOM	Q9Z832.
OMA	TPHSRIM.
Enzyme and pathway databases
BioCyc	CPNE115711:CP_0233-MON. CPNE115713:CPN0520-MON. CPNE138677:CPJ0520-MON. CPNE182082:CPB0541-MON.
BRENDA	3.4.21.92. 264832.
Family and domain databases
HAMAP	MF_00444. [Tree]
InterPro	IPR001907. Pept_S14_ClpP. IPR018215. Pept_S14_ClpP_AS. [Graphical view]
PANTHER	PTHR10381. Pept_S14_ClpP. 1 hit.
Pfam	PF00574. CLP_protease. 1 hit. [Graphical view]
PRINTS	PR00127. CLPPROTEASEP.
PROSITE	PS00382. CLP_PROTEASE_HIS. 1 hit. PS00381. CLP_PROTEASE_SER. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CLPP1_CHLPN

Accession

Primary (citable) accession number: Q9Z832
Secondary accession number(s): Q9JQ83

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)