Protein Family Models

This domain is found in Sensor protein TorS from Escherichia coli and similar proteins predominantly found in proteobacteria. TorS is a sensor histidine kinase that forms a complex with TorT, and TorR, to form the trimethylamine-N-oxide (TMAO) reductase (Tor) pathway, which plays a role in the regulation of this terminal electron receptor in anaerobic respiration. This domain folds into a four-helical bundle [1-3]. Paper describing PDB structure 3i9w. [1]. 19748340. Structural analysis of sensor domains from the TMAO-responsive histidine kinase receptor TorS. Moore JO, Hendrickson WA;. Structure. 2009;17:1195-1204. Paper describing PDB structure 3o1h. [2]. 22483119. An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO. Moore JO, Hendrickson WA;. Structure. 2012;20:729-741. (from Pfam)

Date:

2024-10-16

TorS histidine kinase activates the TMAO reductase (Tor) pathway when sensing trimethylamine-N-oxide (TMAO) in the environment. This entry represents the N-terminal portion of the periplasmic sensor domains of TorS. Paper describing PDB structure 3i9w. [1]. 19748340. Structural analysis of sensor domains from the TMAO-responsive histidine kinase receptor TorS. Moore JO, Hendrickson WA;. Structure. 2009;17:1195-1204. Paper describing PDB structure 3o1h. [2]. 22483119. An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO. Moore JO, Hendrickson WA;. Structure. 2012;20:729-741. (from Pfam)

Date:

2024-10-16

This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90. [1]. 18361456. Crystal structure of a novel non-Pfam protein AF1514 from Archeoglobus fulgidus DSM 4304 solved by S-SAD using a Cr X-ray source. Li Y, Bahti P, Shaw N, Song G, Chen S, Zhang X, Zhang M, Cheng C, Yin J, Zhu JY, Zhang H, Che D, Xu H, Abbas A, Wang BC, Liu ZJ;. Proteins 2008;71:2109-13. (from Pfam)

Date:

2024-10-16

The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined [1]. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein Pfam:PF00072) [2]. [1]. 9054511. Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. Kato M, Mizuno T, Shimizu T, Hakoshima T;. Cell 1997;88:717-723. [2]. 12582120. Ssk1p response regulator binding surface on histidine- containing phosphotransfer protein ypd1p. Porter SW, Xu Q, West AH;. Eukaryot Cell 2003;2:27-33. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Dimerisation and phospho-acceptor domain of histidine kinases. [1]. 9989504. Structure of CheA, a signal-transducing histidine kinase. Bilwes AM, Alex LA, Crane BR, Simon MI;. Cell 1999;96:131-141. [2]. 18361456. Crystal structure of a novel non-Pfam protein AF1514 from Archeoglobus fulgidus DSM 4304 solved by S-SAD using a Cr X-ray source. Li Y, Bahti P, Shaw N, Song G, Chen S, Zhang X, Zhang M, Cheng C, Yin J, Zhu JY, Zhang H, Che D, Xu H, Abbas A, Wang BC, Liu ZJ;. Proteins 2008;71:2109-13. (from Pfam)

Date:

2024-10-16

This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain. [1]. 7699720. Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution. Pao GM, Saier MH;. J Mol Evol 1995;40:136-154. (from Pfam)

Date:

2024-10-16

This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (PF02518), HAMP (PF00672), phosphoacceptor (PF00512), and phosphotransfer (PF01627) domains and a response regulator receiver domain (PF00072).

Gene:

torS

Date:

2024-05-13