Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone.
Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease.
Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth.
Large-scale identification of protein-protein interaction of Escherichia coli K-12.
Protein abundance profiling of the Escherichia coli cytosol.
Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage.
Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry.
ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics.
Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
The interplay of ClpXP with the cell division machinery in Escherichia coli.
ClpX(P) generates mechanical force to unfold and translocate its protein substrates.
Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine.
The binary protein-protein interaction landscape of Escherichia coli.
Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX.
Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli.
The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system.
Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP.
Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.
Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation.
UniProt entry P0A6H1 (CLPX_ECOLI)