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

molecular chaperone HscA is involved in the maturation of iron-sulfur cluster-containing proteins, its ATPase activity is stimulated by HscB

Date:

2023-02-22

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

Gene:

hscA

Date:

2020-10-26

The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK.

Gene:

hscA

Date:

2024-05-30