Protein Family Models

This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl [1]. [1]. 12758091. Cytoskeletons in prokaryotes. Mayer F;. Cell Biol Int 2003;27:429-438. (from Pfam)

Date:

2024-10-16

Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region. [1]. 9476895. The Hsp70 and Hsp60 chaperone machines. Bukau B, Horwich AL;. Cell 1998;92:351-366. (from Pfam)

Date:

2024-10-16

Involved in the maturation of iron-sulfur cluster-containing proteins

Gene:

hscA

Date:

2020-10-26

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

Gene:

dnaK

Date:

2021-07-21

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

Date:

2024-07-11

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.

Gene:

dnaK

Date:

2024-07-09