Protein Family Models

Members of this family adopt a secondary structure consisting of an open-face beta/alpha sandwich, with four antiparallel beta-strands and two alpha-helices. They bind to a corresponding domain on CheY, with subsequent phosphorylation of the CheY Asp57 residue, and activation of CheY, which then affects flagellar rotation [1]. [1]. 11134926. Further insights into the mechanism of function of the response. regulator CheY from crystallographic studies of the. CheY--CheA(124--257) complex.. Gouet P, Chinardet N, Welch M, Guillet V, Cabantous S, Birck C,. Mourey L, Samama JP;. Acta Crystallogr D Biol Crystallogr. 2001;57:44-51. (from Pfam)

Date:

2024-08-14

This helical bundle domain is the homodimer interface of the signal transducing histidine kinase family. [1]. 9989504. Structure of CheA, a signal-transducing histidine kinase.. Bilwes AM, Alex LA, Crane BR, Simon MI;. Cell 1999;96:131-141. (from Pfam)

Date:

2024-08-14

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:

2024-08-14

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:

2024-08-14

CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA [1] binds to CheW, suggesting that these domains can interact with each other. [1]. 9989504. Structure of CheA, a signal-transducing histidine kinase.. Bilwes AM, Alex LA, Crane BR, Simon MI;. Cell 1999;96:131-141. (from Pfam)

Date:

2024-08-14

chemotaxis protein CheA is a sensor histitine protein kinase that transmits sensory signals from chemoreceptors to the flagellar motors

Date:

2018-03-14

Chemotactic sensory histidine kinase in two-component regulatory system with CheB and CheY; sensory histidine kinase/signal sensing protein; CheA is the histidine kinase component

Gene:

cheA

Date:

2021-08-24