Strain |
Pseudomonas aeruginosa PAO1 (Stover et al., 2000)
GCF_000006765.1|latest |
Locus Tag |
PA1801
|
Name |
clpP
|
Replicon | chromosome |
Genomic location | 1954069 - 1954710 (+ strand) |
Transposon Mutants | 1 transposon mutants in PAO1 |
Transposon Mutants in orthologs | 1 transposon mutants in orthologs |
RefSeq | NP_250492.1 |
GI | 15596998 |
Affymetrix | PA1801_clpP_at |
DNASU | PaCD00006820 |
Entrez | 878359 |
GenBank | AAG05190.1 |
INSDC | AAG05190.1 |
NCBI Locus Tag | PA1801 |
protein_id(GenBank) | gb|AAG05190.1|AE004606_4|gnl|PseudoCAP|PA1801 |
TIGR | NTL03PA01802 |
UniParc | UPI0000127AE8 |
UniProtKB Acc | Q9I2U1 |
UniProtKB ID | CLPP1_PSEAE |
UniRef100 | UniRef100_Q9I2U1 |
UniRef50 | UniRef50_Q9I2U1 |
UniRef90 | UniRef90_Q9I2U1 |
Feature Type | CDS |
Coding Frame | 1 |
Product Name |
ClpP
|
Synonyms |
protease ti |
Evidence for Translation |
Detected by MALDI-TOF/TOF (PMID:19333994).
Identified using nanoflow high-pressure liquid chromatography (HPLC) in conjunction with microelectrospray ionization on LTQ XL mass spectrometer (PMID:24291602).
|
Charge (pH 7) | -2.42 |
Kyte-Doolittle Hydrophobicity Value | -0.017 |
Molecular Weight (kDa) | 23.5 |
Isoelectric Point (pI) | 6.39 |
Individual Mappings | |
Additional evidence for subcellular localization |
Accession | Header | Accession Date | Compound | Source | Resolution | Method | Percent Identity |
7M1M | HYDROLASE | 03/13/21 | Crystal structure of Pseudomonas aeruginosa ClpP1 | Pseudomonas aeruginosa | 2.6 | X-RAY DIFFRACTION | 100.0 |
Results |
Common
Found in both pathogen and nonpathogenic strains
Hits to this gene were found in 582 genera
|
Pseudomonas Ortholog Database | View orthologs at Pseudomonas Ortholog Database |
Pseudomonas Ortholog Group |
POG003596 (535 members) |
Putative Inparalogs | None Found |
STRING database | Search for predicted protein-protein interactions using:
Search term: PA1801
Search term: clpP
Search term: ClpP
|
Ensembl
110, assembly
GRCh38.p14
|
caseinolytic mitochondrial matrix peptidase proteolytic subunit [Source:HGNC Symbol;Acc:HGNC:2084]
E-value:
4.7e-60
Percent Identity:
59.0
|
The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.
Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B, Georgopoulos C, Zylicz M
EMBO J 1995 May 1;14(9):1867-77
PubMed ID: 7743994
|
Molecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome.
Shin DH, Lee CS, Chung CH, Suh SW
J Mol Biol 1996 Sep 20;262(2):71-6
PubMed ID: 8831780
|
Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP.
Grimaud R, Kessel M, Beuron F, Steven AC, Maurizi MR
J Biol Chem 1998 May 15;273(20):12476-81
PubMed ID: 9575205
|
ClpXP proteases positively regulate alginate overexpression and mucoid conversion in Pseudomonas aeruginosa.
Qiu D, Eisinger VM, Head NE, Pier GB, Yu HD
Microbiology (Reading) 2008 Jul;154(Pt 7):2119-2130
PubMed ID: 18599839
|
Analysis of the periplasmic proteome of Pseudomonas aeruginosa, a metabolically versatile opportunistic pathogen.
Imperi F, Ciccosanti F, Perdomo AB, Tiburzi F, Mancone C, Alonzi T, Ascenzi P, Piacentini M, Visca P, Fimia GM
Proteomics 2009 Apr;9(7):1901-15
PubMed ID: 19333994
|
Role of intracellular proteases in the antibiotic resistance, motility, and biofilm formation of Pseudomonas aeruginosa.
Fernández L, Breidenstein EB, Song D, Hancock RE
Antimicrob Agents Chemother 2012 Feb;56(2):1128-32
PubMed ID: 22123702
|