Protein Family Models

This domain is found in a wide variety of bacterial signalling proteins. It is likely to be a transmembrane domain involved in ligand sensing. (from Pfam)

Date:

2024-08-14

This entry represents an N-terminal domain found in KdpD sensor kinase proteins that regulate the kdpFABC operon responsible for potassium transport [1]. The aligned region corresponds to a cytoplasmic part of the protein which functions as the sensor domain responsible for sensing turgor pressure [2]. It recognises C-di-AMP and K+ [3]. [1]. 9226259. The kdp system of Clostridium acetobutylicum: cloning, sequencing, and transcriptional regulation in response to potassium concentration. Treuner-Lange A, Kuhn A, Durre P;. J Bacteriol 1997;179:4501-4512. [2]. 1532388. KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators. Walderhaug MO, Polarek JW, Voelkner P, Daniel JM, Hesse JE, Altendorf K, Epstein W;. J Bacteriol 1992;174:2152-2159. [3]. 34424339. A catalogue of signal molecules that interact with sensor kinases, chemoreceptors and transcriptional regulators. Matilla MA, Velando F, Martin-Mora D, Monteagudo-Cascales E, Krell T;. FEMS Microbiol Rev. 2022;46:fuab043. (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 universal stress protein UspA Swiss:P28242 [1] is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA [3] reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP [2], though UspA lacks ATP-binding activity. [1]. 8152377. Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest. Nystrom T, Neidhardt FC;. Mol Microbiol 1994;11:537-544. [2]. 9860944. Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics. Zarembinski TI, Hung LW, Mueller-Dieckmann HJ, Kim KK, Yokota H, Kim R, Kim SH;. Proc Natl Acad Sci U S A 1998;95:15189-15193. [3]. 11738040. Structure of the universal stress protein of Haemophilus influenzae. Sousa MC, McKay DB;. Structure (Camb) 2001;9:1135-1141. (from Pfam)

Date:

2024-10-16

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

sensor histidine kinase, part of a two-component regulatory system, functions as a protein kinase that phosphorylates a target protein in response to various signals

Date:

2024-04-17