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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0498 IGR0497 IGR0496 IGR0495 IGR0499 IGR0500 IGR0494 IGR0494.1 ndk, - NG0597 NG0591 pilF, - NG0595 NG0596 NG0598 gcpE,ispG, - NG0594 clpP, - NG0593 tig, - NG0592 ftsK,spoIIIE, - NG0590 ndk, - NG0597 NG0591 pilF, - NG0595 NG0596 NG0598 gcpE,ispG, - NG0594 clpP, - NG0593 tig, - NG0592 ftsK,spoIIIE, - NG0590 Type: inverse, Name:  - 167 ndk, - NG0597 NG0591 pilF, - NG0595 NG0596 NG0598 gcpE,ispG, - NG0594 clpP, - NG0593 tig, - NG0592 ftsK,spoIIIE, - NG0590
* Calculated from Protein Sequence

Gene ID: NG0593

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
clpP  

Definition:
ATP-dependent Clp protease, proteolytic subunit

Gene Start:
580178

Gene Stop:
580789

Gene Length:
612

Molecular Weight*:
22591

pI*:
5.20

Net Charge*:
-5.12

EC:
3.4.21.92  

Functional Class:
Translation; Degradation of proteins, peptides, and glycopeptides  

Pathway: pathway table

Secondary Evidence:
Maurizi,M.R., Clark,W.P., Katayama,Y., Rudikoff,S., Pumphrey,J.,Bowers,B. and Gottesman,S. Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 265 (21): 12536-12545 (1990) [Medline: 90324245].

Kroh,H.E. and Simon,L.D. The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5. J. Bacteriol. 172 (10): 6026-6034 (1990) [Medline: 91008981].

Arribas,J. and Castano,J.G. A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli. J. Biol. Chem. 268 (28): 21165-21171 (1993) [Medline: 94012667].

Shin,D.H., Lee,C.S., Chung,C.H. and Suh,S.W. Molecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome. J. Mol. Biol. 262 (2): 71-76 (1996) [Medline: 96428678].

Wang,J., Hartling,J.A. and Flanagan,J.M. The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Cell 91 (4): 447-456 (1997) [Medline: 98050920].

Comment:
For other 'clp' genes, see NG0408 (clpA), NG0645 (clpX), NG1046 (clpB).

From GenBANK (gi:116523): In E. coli, this protein cleaves peptides in various proteins in a process that requires ATP hydrolysis. It has a chymotrypsin-like activity and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. ClpP may play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Its catalytic activity is the 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 cleaved (such as succinyl-leu-tyr-|-nhmec; and leu-tyr-leu-|-tyr-trp, in which the cleavage of the -tyr-|-leu-and -tyr-|-trp- bond also occurs). Twelve ClpP subunits assemble into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. In the presence of ATP, ClpA or ClpX subunits interact with the ClpP structure to form a 750 kda complex that
exhibits ATP-dependent proteolytic activity. Also, this protein is induced by heat shock.

See also ClpX, NG0645.

Oklahoma ID: NGO.593

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST; e.g. residues 7-199 are 72% similar to dbj|BAB33914.1| (AP002551) ATP-dependent proteolytic subunit of clpA-clpP serine protease ClpP of Escherichia coli O157:H7.

Residues 1-204 are 99% similar to NMA1525, endopeptidase of N.meningitidis (11265177). Residues 29-204 are 98% similar to NMB1312, ATP-dependent Clp proteinase of N.meningitidis (11265158). Also 73% similar to NMB1312, ATP-dependent Clp proteinase of N.meningitidis (11265158).

COGS Summary:  COGS Search
BeTs to 11 clades of COG0740
COG name: Protease subunits of ATP-dependent proteases, ClpP family
Functional Class:  O
The phylogenetic pattern of COG0740 is -----qvCebRhuj--OLINx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001907 (Clp protease) with a combined E-value of 3.3e-118.
    IPB001907A    8-32
    IPB001907B    48-93
    IPB001907C    94-132
    IPB001907D    152-195


ProDom Summary:  Protein Domain Search
Residues 8-196 are 72% similar to a (PROTEASE CLP HYDROLASE ENDOPEPTIDASE SERINE) protein domain (PD001650) which is seen in CLPP_ECOLI.



Paralogs:  Local Blast Search


NG0593 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 16 to 199 (E-value = 3.7e-137) place NG0593 in the CLP_protease family which is described as Clp protease (PF00574)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
139  
174

PDB Hit:
pdb|1TYF|1TYF-A THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION353.0 2e-98

Gene Protein Sequence:
MSFDNHLVPTVIEQSGRGERAFDIYSRLLKERIVFLVGPVTDESANLVVA
QLLFLESENPDKDIFFYINSPGGSVTAGMSIYDTMNFIKPDVSTLCLGQA
ASMGAFLLSAGEKGKRFALPNSRIMIHQPLISGGLGGQASDIEIHARELL
KIKEKLNRLMAKHCGRDLADLERDTDRDNFMSAEEAKEYGLIDQVLENRA
SLRL

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCTTTTGATAACCATCTTGTCCCTACCGTTATCGAGCAGAGCGGTCG
CGGTGAGCGTGCATTCGATATCTATTCCCGGCTTTTGAAAGAGCGCATCG
TATTTCTGGTTGGCCCGGTAACCGATGAGTCTGCTAATCTGGTGGTCGCC
CAACTGTTGTTTTTGGAAAGTGAGAATCCGGATAAGGATATTTTCTTCTA
CATCAATTCCCCCGGCGGCTCGGTAACGGCCGGTATGTCGATTTACGACA
CGATGAATTTCATCAAGCCCGATGTATCGACTTTGTGCTTGGGGCAGGCG
GCAAGTATGGGCGCGTTCTTATTGTCGGCAGGCGAGAAAGGCAAACGTTT
CGCCCTGCCCAACAGCCGGATTATGATTCACCAGCCTTTAATCAGCGGCG
GCTTGGGCGGTCAGGCATCCGACATTGAAATCCACGCACGCGAGTTGTTG
AAAATCAAAGAAAAACTCAACCGCCTGATGGCGAAACATTGCGGCCGCGA
TTTGGCAGATTTGGAGCGCGACACCGACCGTGATAATTTCATGTCTGCCG
AAGAAGCAAAAGAATATGGTTTGATCGACCAAGTTTTGGAAAACCGCGCT
TCTTTGCGGCTT


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