Summary: ATP-dependent Clp protease adaptor protein ClpS
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This is the Wikipedia entry entitled "ATP-dependent Clp protease adaptor protein ClpS". More...
ATP-dependent Clp protease adaptor protein ClpS Edit Wikipedia article
ClpS | |||||||||
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Identifiers | |||||||||
Symbol | ClpS | ||||||||
Pfam | PF02617 | ||||||||
InterPro | IPR003769 | ||||||||
SCOPe | 1mbx / SUPFAM | ||||||||
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ClpS is an N-recognin in the N-end rule pathway.[1] ClpS interacts with protein substrates that have a bulky hydrophobic residue (leucine, phenylalanine, tyrosine, and tryptophan) at the N-terminus. The protein substrate is then degraded by the ClpAP protease.[2][3]
In molecular biology, the ATP-dependent Clp protease adaptor protein ClpS is a bacterial protein. In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins.[4]
ClpS is a small alpha/beta protein that consists of three alpha-helices connected to three antiparallel beta-strands.[5] The protein has a globular shape, with a curved layer of three antiparallel alpha-helices over a twisted antiparallel beta-sheet. Dimerization of ClpS may occur through its N-terminal domain. This short extended N-terminal region in ClpS is followed by the central seven-residue beta-strand, which is flanked by two other beta-strands in a small beta-sheet.
See also
References
- ^ Varshavsky, Alexander (2011-08-01). "The N-end rule pathway and regulation by proteolysis". Protein Science. 20 (8): 1298–1345. doi:10.1002/pro.666. ISSN 1469-896X. PMC 3189519. PMID 21633985.
- ^ Tasaki T, Sriram SM, Park KS, Kwon YT (10 April 2012). "The N-end rule pathway". Annu Rev Biochem. 81: 261–289. doi:10.1146/annurev-biochem-051710-093308. PMC 3610525. PMID 22524314.
- ^ Erbse, A.; Schmidt, R.; Bornemann, T.; Schneider-Mergener, J.; Mogk, A.; Zahn, R.; Dougan, D. A.; Bukau, B. (2006). "ClpS is an essential component of the N-end rule pathway in Escherichia coli". Nature. 439 (7077): 753–756. doi:10.1038/nature04412. PMID 16467841.
- ^ Dougan DA, Reid BG, Horwich AL, Bukau B (March 2002). "ClpS, a substrate modulator of the ClpAP machine". Mol. Cell. 9 (3): 673–83. doi:10.1016/S1097-2765(02)00485-9. PMID 11931773.
- ^ Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA (December 2002). "Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA". Nat. Struct. Biol. 9 (12): 906–11. doi:10.1038/nsb869. PMID 12426582.
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ATP-dependent Clp protease adaptor protein ClpS Provide feedback
In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins [1].
Literature references
-
Dougan DA, Reid BG, Horwich AL, Bukau B; , Mol Cell 2002;9:673-683.: ClpS, a substrate modulator of the ClpAP machine. PUBMED:11931773 EPMC:11931773
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Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA; , Nat Struct Biol 2002;9:906-911.: Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. PUBMED:12426582 EPMC:12426582
External database links
SCOP: | 1mbx |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003769
In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins [PUBMED:11931773].
ClpS is a small alpha/beta protein that consists of three alpha-helices connected to three antiparallel beta-strands [PUBMED:12426582]. The protein has a globular shape, with a curved layer of three antiparallel alpha-helices over a twisted antiparallel beta-sheet. Dimerization of ClpS may occur through its N-terminal domain. This short extended N-terminal region in ClpS is followed by the central seven-residue beta-strand, which is flanked by two other beta-strands in a small beta-sheet.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Biological process | protein catabolic process (GO:0030163) |
Domain organisation
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Seed (259) |
Full (6451) |
Representative proteomes | UniProt (24014) |
NCBI (24835) |
Meta (1063) |
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RP15 (699) |
RP35 (2541) |
RP55 (5342) |
RP75 (9161) |
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PP/heatmap | 1 |
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Seed (259) |
Full (6451) |
Representative proteomes | UniProt (24014) |
NCBI (24835) |
Meta (1063) |
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---|---|---|---|---|---|---|---|---|---|
RP15 (699) |
RP35 (2541) |
RP55 (5342) |
RP75 (9161) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Curation
Seed source: | COG2127 |
Previous IDs: | DUF174; |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Mian N |
Number in seed: | 259 |
Number in full: | 6451 |
Average length of the domain: | 76.60 aa |
Average identity of full alignment: | 29 % |
Average coverage of the sequence by the domain: | 17.66 % |
HMM information
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model length: | 80 | ||||||||||||
Family (HMM) version: | 18 | ||||||||||||
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ClpS domain has been found. There are 61 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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