Protein Family Models

Date:

2024-08-14

This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport [1,2,3]. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043). [1]. 2651410. Nucleotide sequences of the fecBCDE genes and locations of the. proteins suggest a periplasmic-binding-protein-dependent. transport mechanism for iron(III) dicitrate in Escherichia coli.. Staudenmaier H, Van Hove B, Yaraghi Z, Braun V;. J Bacteriol 1989;171:2626-2633.. [2]. 12475936. The structure of Escherichia coli BtuF and binding to its. cognate ATP binding cassette transporter.. Borths EL, Locher KP, Lee AT, Rees DC;. Proc Natl Acad Sci U S A. 2002;99:16642-16647.. [3]. 14514690. The role of FhuD2 in iron(III)-hydroxamate transport in. Staphylococcus aureus. Demonstration that FhuD2 binds. iron(III)-hydroxamates but with minimal conformational change. and implication of mutations on transport.. Sebulsky MT, Shilton BH, Speziali CD, Heinrichs DE;. J Biol Chem. 2003;278:49890-49900. (from Pfam)

Date:

2024-08-14

In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (Pfam:PF00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerisation domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilised when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added [1-2]. [1]. 9600836. Apo-AraC actively seeks to loop.. Seabold RR, Schleif RF;. J Mol Biol 1998;278:529-538.. [2]. 9600837. Arm-domain interactions in AraC.. Saviola B, Seabold R, Schleif RF;. J Mol Biol 1998;278:539-548. (from Pfam)

Date:

2024-08-14

AraC family transcriptional regulator containing an AraC family helix-turn-helix (HTH) DNA-binding domain and a TroA-like periplasmic binding domain, similar to Bacillus subtilis HTH-type transcriptional activator Btr that activates expression of the feuABCybbA operon, which encodes the bacillibactin uptake system, in iron-limited conditions

Date:

2019-10-25