P0AFA2 · NARX_ECOLI

Function

function

Acts as a sensor for nitrate/nitrite and transduces signal of nitrate availability to the NarL protein and of both nitrate/nitrite to the NarP protein. NarX probably activates NarL and NarP by phosphorylation in the presence of nitrate. NarX also plays a negative role in controlling NarL activity, probably through dephosphorylation in the absence of nitrate.

Catalytic activity

  • ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
    EC:2.7.13.3 (UniProtKB | ENZYME | Rhea)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentouter membrane-bounded periplasmic space
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionphosphoprotein phosphatase activity
Molecular Functionphosphorelay sensor kinase activity
Molecular Functionprotein homodimerization activity
Biological Processcellular response to nitrate
Biological Processcellular response to nitrite
Biological ProcessDNA damage response
Biological Processnitrate assimilation
Biological Processsignal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nitrate/nitrite sensor protein NarX
  • EC number

Gene names

    • Name
      narX
    • Synonyms
      narR
    • Ordered locus names
      b1222, JW1213

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
    • K12 / MC4100 / ATCC 35695 / DSM 6574
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0AFA2
  • Secondary accessions
    • P10956

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-14Cytoplasmic
Transmembrane15-37Helical
Topological domain38-151Periplasmic
Transmembrane152-174Helical
Topological domain175-598Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000748121-598Nitrate/nitrite sensor protein NarX
Modified residue399Phosphohistidine; by autocatalysis

Keywords

Proteomic databases

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P0AFA2narL P0AF282EBI-1112775, EBI-1122899

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain176-228HAMP
Domain393-587Histidine kinase

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    598
  • Mass (Da)
    67,084
  • Last updated
    2005-12-20 v1
  • Checksum
    886BA0FC2C8F3C3E
MLKRCLSPLTLVNQVALIVLLSTAIGLAGMAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNELIPALMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFMALLLVFTIIWLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEHKNQILSFLWQANRRLHSRAPLCERLSPVLNGLQNLTLLRDIELRVYDTDDEENHQEFTCQPDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLADSHTQYGILLATLPQGRHLSHDQQQLVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPALEASCEEYSAKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHSQASEVVVTVAQNDNQVKLTVQDNGCGVPENAIRSNHYGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTFTDVQGDTHE

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict42-52in Ref. 1 and 5
Sequence conflict374in Ref. 6; AAA24198

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X13360
EMBL· GenBank· DDBJ
CAA31741.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC74306.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA36090.1
EMBL· GenBank· DDBJ
Genomic DNA
X15996
EMBL· GenBank· DDBJ
CAA34125.1
EMBL· GenBank· DDBJ
Genomic DNA
M24910
EMBL· GenBank· DDBJ
AAA24198.1
EMBL· GenBank· DDBJ
Genomic DNA
X65715
EMBL· GenBank· DDBJ
CAA46631.1
EMBL· GenBank· DDBJ
Genomic DNA
X69189
EMBL· GenBank· DDBJ
CAA48934.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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