A0A081V5Q8 · A0A081V5Q8_BURCE

Function

function

Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).

Miscellaneous

Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site146
Binding site161-168ATP (UniProtKB | ChEBI)
Active site167
Binding site168Mg2+ (UniProtKB | ChEBI)
Active site185Proton acceptor; for phosphorylation activity. Proton donor; for dephosphorylation activity
Binding site210Mg2+ (UniProtKB | ChEBI)
Active site250

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionphosphorelay sensor kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionprotein serine/threonine/tyrosine kinase activity
Biological Processregulation of carbohydrate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    HPr kinase/phosphorylase
  • EC number
  • Short names
    HPrK/P
  • Alternative names
    • HPr(Ser) kinase/phosphorylase

Gene names

    • Name
      hprK
    • ORF names
      DPR02_04615
      , E3D38_18935
      , JAO13_24135
      , NCTC10661_04088
      , QDD67_002054
      , QZM77_34320
      , VL15_16875
      , WS90_34915
      , WT26_18465

Organism names

  • Taxonomic identifier
  • Strains
    • 871
    • 3285
    • LK29
    • MSMB1302
    • MSMB1184WGS
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex

Accessions

  • Primary accession
    A0A081V5Q8
  • Secondary accessions
    • A0A1I0LI70

Proteomes

Subcellular Location

Interaction

Subunit

Homohexamer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain8-135HPr(Ser) kinase/phosphorylase N-terminal
Domain139-305HPr kinase/phosphorylase C-terminal
Region209-218Important for the catalytic mechanism of both phosphorylation and dephosphorylation
Region271-276Important for the catalytic mechanism of dephosphorylation

Domain

The Walker A ATP-binding motif also binds Pi and PPi.

Sequence similarities

Belongs to the HPrK/P family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    322
  • Mass (Da)
    35,121
  • Last updated
    2014-10-29 v1
  • Checksum
    3E5897176FE2092C
MDTSSINAQSIFDDNAATLKLSWLTGHEGWERGFSADTVGNATSSADLVGHLNLIHPNRIQVLGEAEIDYYQRQTDEDRSRHMAELIALEPPFLVVAGGAAAPPELVLRCTRSSTPLFTTPMSAAAVIDSLRLYMSRILAPRATLHGVFIDILGMGVLLTGDSGLGKSELGLELISRGHGLVADDAVDFVRLGPDFVEGRCPPLLQNLLEVRGLGLLDIKTIFGETAVRRKMKLKLIVQLVRRPDGEFQRLPLESQTVDVLGLPISKVTIQVAAGRNLAVLVEAAVRNTILQLRGIDTLRDFMDRQRLAMQDPDSQFPGKLV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP013443
EMBL· GenBank· DDBJ
AOK17803.1
EMBL· GenBank· DDBJ
Genomic DNA
ABLMVR010000007
EMBL· GenBank· DDBJ
EKS9795308.1
EMBL· GenBank· DDBJ
Genomic DNA
LDWR01000028
EMBL· GenBank· DDBJ
KML56134.1
EMBL· GenBank· DDBJ
Genomic DNA
LOYH01000108
EMBL· GenBank· DDBJ
KVK72086.1
EMBL· GenBank· DDBJ
Genomic DNA
JAEDXG010000024
EMBL· GenBank· DDBJ
MBH9699537.1
EMBL· GenBank· DDBJ
Genomic DNA
JAUJSP010000031
EMBL· GenBank· DDBJ
MDN7915337.1
EMBL· GenBank· DDBJ
Genomic DNA
QLUZ01000002
EMBL· GenBank· DDBJ
RAQ15280.1
EMBL· GenBank· DDBJ
Genomic DNA
UARD01000023
EMBL· GenBank· DDBJ
SPV20722.1
EMBL· GenBank· DDBJ
Genomic DNA
SNSP01000023
EMBL· GenBank· DDBJ
TEU50259.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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