P37313 · DPPF_ECOLI

  • Protein
    Dipeptide transport ATP-binding protein DppF
  • Gene
    dppF
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Part of the ABC transporter DppABCDF involved in dipeptide transport (PubMed:7536291).
Responsible for energy coupling to the transport system (Probable)
When a foreign outer membrane heme receptor is expressed in E.coli, DppABCDF can also transport heme and its precursor, 5-aminolevulinic acid (ALA), from the periplasm into the cytoplasm.

Catalytic activity

Features

Showing features for binding site.

133450100150200250300
TypeIDPosition(s)Description
Binding site55-62ATP (UniProtKB | ChEBI)

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 ComponentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functiondipeptide transmembrane transporter activity
Molecular Functionheme transmembrane transporter activity
Biological Processdipeptide transport
Biological Processheme transmembrane transport
Biological Processpeptide transport
Biological Processprotein transport
Biological Processresponse to radiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dipeptide transport ATP-binding protein DppF
  • EC number

Gene names

    • Name
      dppF
    • Synonyms
      dppE
    • Ordered locus names
      b3540, JW3509

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / MM500
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P37313
  • Secondary accessions
    • Q2M7K2

Proteomes

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Inactivation of the gene abolishes use of heme as an iron source.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000923171-334Dipeptide transport ATP-binding protein DppF

Proteomic databases

Interaction

Subunit

The complex is composed of two ATP-binding proteins (DppD and DppF), two transmembrane proteins (DppB and DppC) and a solute-binding protein (DppA) (PubMed:16905647, PubMed:7536291).
MppA can replace DppA as binding protein for heme and ALA transport (PubMed:16905647).
View interactors in UniProtKB
View CPX-4345 in Complex Portal

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain13-262ABC transporter

Sequence similarities

Belongs to the ABC transporter superfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    334
  • Mass (Da)
    37,560
  • Last updated
    1994-10-01 v1
  • Checksum
    4E5619914955CA51
MSTQEATLQQPLLQAIDLKKHYPVKKGMFAPERLVKALDGVSFNLERGKTLAVVGESGCGKSTLGRLLTMIEMPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSKEQRREKALSMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKDQIFNNPRHPYTQALLSATPRLNPDDRRERIKLSGELPSPLNPPPGCAFNARCRRRFGPCTQLQPQLKDYGGQLVACFAVDQDENPQR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict320-334in Ref. 1; AAA23706

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L08399
EMBL· GenBank· DDBJ
AAA23706.1
EMBL· GenBank· DDBJ
Genomic DNA
U00039
EMBL· GenBank· DDBJ
AAB18518.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76565.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77754.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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