Protein Family Models

This domain is associated to sensor histidine kinases and recognises citrate and TCA cycle intermediates, Ag(II), Zn(II), Mg(II) (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 27049771. Cache Domains That are Homologous to, but Different from PAS Domains Comprise the Largest Superfamily of Extracellular Sensors in Prokaryotes. Upadhyay AA, Fleetwood AD, Adebali O, Finn RD, Zhulin IB;. PLoS Comput Biol. 2016;12:e1004862. (from Pfam)

Date:

2024-10-16

Sporulation initiation phospho-transferase B or SpoOB is part of a phospho-relay that initiates sporulation in Bacillus subtilis. Spo0B is a two-domain protein consisting of an N-terminal alpha-helical hairpin domain and a C-terminal alpha/beta domain. Two subunits of Spo0B dimerise by a parallel association of helical hairpins to form a novel four-helix bundle from which the active histidine - involved in the auto-phosphorylation - protrudes. In the phospho-relay, the signal-receptor histidine kinases are dephosphorylated by a common response regulator, Spo0F. Spo0B then takes phosphorylated Spo0F as substrate thereby mediating the transfer of a phosphoryl group to Spo0A, the ultimate transcription factor. The exact function of this alpha-helical domain is not known; it does not always occur just as the N-terminal domain of SPOB_ab, Pfam:PF14682. SCOP describes this domain as a histidine kinase-like fold lacking the kinase ATP-binding site. [1]. 9809070. Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase. Varughese KI, Madhusudan, Zhou XZ, Whiteley JM, Hoch JA;. Mol Cell. 1998;2:485-493. (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 PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs [4]. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 9301332. PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox. Zhulin IB, Taylor BL, Dixon R;. Trends Biochem Sci 1997;22:331-333. [2]. 7756254. 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Borgstahl GE, Williams DR, Getzoff ED;. Biochemistry 1995;34:6278-6287. [3]. 9382818. PAS: a multifunctional domain family comes to light. Ponting CP, Aravind L;. Curr Biol 1997;7:674-677. [4]. 15009198. The PAS fold: a redefination of the PAS domain based upon structural prediction. Hefti MH, Francoijs KJ, de Vries SC, Dixon R, Vervoort J;. Eur J Biochem 2004;271:1198-1208. (from Pfam)

Date:

2024-10-16

DcuS, as found in Escherichia coli, is a C4-dicarboxylate-sensing histidine kinase, part of a two-component regulatory system with DcuR. It regulates anaerobic fumarate respiration. MalK, as found in Bacillus subtilis, is a malate sensor histidine kinase.

Gene:

dcuS

Date:

2022-02-18

two-component system sensor histidine kinase with a PAS sensor and/or ligand binding domain functions as a protein kinase that phosphorylates a target protein in response to various signals, similar to Escherichia coli sensor histidine kinase DcuS and Bacillus subtilis sensor histidine kinase MalK

Date:

2019-06-19