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Literature summary for 2.7.13.3 extracted from

  • Khorchid, A.; Ikura, M.
    Bacterial histidine kinase as signal sensor and transducer (2006), Int. J. Biochem. Cell Biol., 38, 307-312.
    View publication on PubMed

Application

Application Comment Organism
medicine significance in pathological virulence of Salmonella enterica, seductive target for anti-bacterial therapeutic development Salmonella enterica
additional information 15 of the 30 known Escherichia coli histidine kinases contain a single HAMP domain, has an important role in signal transduction Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information mutations within the linker HAMP domain block the osmosensing function of EnvZ Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
inner membrane EnvZ with a N-terminal cytoplasmic tail (residues 1-15), two transmembrane domains (residues 16-34 and residues 163-179) flanking a periplasmic domain (residues 48-162), and a cytoplasmic domain (residues 180-450). The cytoplasmic domain can be further dissected into a linker or HAMP domain (residues 180-222), domain A (dimerization and histidine containing domain, residues 223-289) and domain B (catalysis assisting and ATP binding domain, residues 290-450), UhpB contains eight transmembrane segments Escherichia coli
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membrane FixL contains four transmembrane segments Sinorhizobium meliloti 16020
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Salmonella enterica
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Sinorhizobium meliloti
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Synonyms

Synonyms Comment Organism
ENVZ
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Escherichia coli
FixL
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Sinorhizobium meliloti
histidine kinase
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Sinorhizobium meliloti
histidine kinase
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Escherichia coli
histidine kinase
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Salmonella enterica
UhpB
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Escherichia coli