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Fe-S protein assembly chaperone HscA
Involved in the maturation of iron-sulfur cluster-containing proteins
molecular chaperone DnaK
Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE
Hsp70 family protein
Hsp70 (heat shock protein 70) family protein is a molecular chaperone involved in DNA replication, protein folding and the stress response: similar to human hsp70 which is involved in the chaperoning of nascent polypeptides and protection against the accumulation of malfolded proteins
Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved.
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