F
IPR014285

Nitrogen fixation negative regulator NifL

InterPro entry
Short nameN_fixation_neg-reg_NifL

Description

NifL from Azotobacter vinelandii senses both the redox and fixed nitrogen status to regulate nitrogen fixation. NifL acts by modulating the activity of the nitrogen fixation positive regulator protein NifA; NifL inhibits NifA in response to oxygen and low level of fixed nitrogen. NifA and NifL are encoded by adjacent genes. NifL is FAD-containing, and has a domain architecture similar to that of the cytoplasmic histidine protein kinases, containing two N-terminal PAS domains and a C-terminal transmitter region containing a conserved histidine residue (H domain) and a nucleotide binding GHKL domain corresponding to the catalytic core of the histidine kinases
[1]
. However, NifL does not exhibit kinase activity and regulates its partner NifA by direct protein-protein interactions rather than phosphorylation.

References

1.Role of the H domain of the histidine kinase-like protein NifL in signal transmission. Little R, Martinez-Argudo I, Perry S, Dixon R. J. Biol. Chem. 282, 13429-37, (2007). View articlePMID: 17355964

GO terms

molecular function

  • None

cellular component

  • None

Cross References

Contributing Member Database Entry
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