Protein Family Models

This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90. (from Pfam)

Date:

2024-08-14

The PhoQ Sensor is required for the virulence of various Gram-negative bacteria by allowing interaction of PhoPQ with the intracellular membrane, resulting in remodelling of the bacterial cell surface and subsequent bacterial resistance to host antimicrobial peptides. The domain contains a major flat acidic surface, which binds to at least 3 calcium ions, neutralising the domain's negative charge and allowing interaction with the negatively charged membrane [1]. This domain recognises divalent metal cations, and antimicrobial cationic peptides (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 16406409. Metal bridges between the PhoQ sensor domain and the membrane regulate transmembrane signaling. Cho US, Bader MW, Amaya MF, Daley ME, Klevit RE, Miller SI, Xu W;. J Mol Biol. 2006;356:1193-1206. (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

Date:

2024-08-14

two-component system sensor histidine kinase PhoQ is a member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes

Date:

2018-08-23

Gene:

phoQ

Date:

2021-10-15