Q2FDW8 · PTU3C_STAA3

Function

function

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in alpha- and beta-glucoside transport (By similarity).

Features

Showing features for active site.

168850100150200250300350400450500550600650
TypeIDPosition(s)Description
Active site460Phosphocysteine intermediate; for EIIB activity
Active site612Tele-phosphohistidine intermediate; for EIIA activity

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 Componentplasma membrane
Molecular Functionglucose transmembrane transporter activity
Molecular Functionkinase activity
Molecular Functionprotein-N(PI)-phosphohistidine-sugar phosphotransferase activity
Molecular Functionprotein-phosphocysteine-sugar phosphotransferase activity
Biological Processphosphoenolpyruvate-dependent sugar phosphotransferase system
Biological Processphosphorylation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    PTS system glucoside-specific EIICBA component

Including 3 domains:

  • Recommended name
    Glucoside permease IIC component
  • Alternative names
    • PTS system glucoside-specific EIIC component
  • Recommended name
    Glucoside-specific phosphotransferase enzyme IIB component
  • EC number
  • Alternative names
    • PTS system glucoside-specific EIIB component
  • Recommended name
    Glucoside-specific phosphotransferase enzyme IIA component
  • Alternative names
    • PTS system glucoside-specific EIIA component

Gene names

    • Name
      glcB
    • Ordered locus names
      SAUSA300_2476

Organism names

Accessions

  • Primary accession
    Q2FDW8

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-32Helical
Transmembrane81-101Helical
Transmembrane137-157Helical
Transmembrane182-202Helical
Transmembrane223-243Helical
Transmembrane284-304Helical
Transmembrane315-335Helical
Transmembrane340-360Helical
Transmembrane364-384Helical
Transmembrane395-415Helical

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003514081-688PTS system glucoside-specific EIICBA component

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-427PTS EIIC type-1
Domain438-519PTS EIIB type-1
Domain560-664PTS EIIA type-1

Domain

The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    688
  • Mass (Da)
    74,416
  • Last updated
    2006-03-21 v1
  • Checksum
    41C3BF6C9FE718FA
MFKKLFGQLQRIGKALMLPVAILPAAGILLAFGNAMHNEQLVEIAPWLKNDIIVMISSVMEAAGQVVFDNLPLLFAVGTALGLAGGDGVAALAALVGYLIMNATMGKVLHITIDDIFSYAKGAKELSQAAKEPAHALVLGIPTLQTGVFGGIIMGALAAWCYNKFYNITLPPFLGFFAGKRFVPIVTSVVAIATGVLLSFAWPPIQDGLNSLSNFLLNKNLTLTTFIFGIIERSLIPFGLHHIFYSPFWFEFGSYTNHAGELVRGDQRIWMAQLKDGVPFTAGAFTTGKYPFMMFGLPAAAFAIYKNARPERKKVVGGLMLSAGLTAFLTGITEPLEFSFLFVAPVLYGIHVLLAGTSFLVMHLLGVKIGMTFSGGFIDYILYGLLNWDRSHALLVIPVGIVYAIVYYFLFDFAIRKFKLKTPGREDEETEIRNSSVAKLPFDVLDAMGGKENIKHLDACITRLRVEVVDKSKVDVAGIKALGASGVLEVGNNMQAIFGPKSDQIKHDMAKIMSGEITKPSETTVTEEMSDEPVHVEALGTTDIYAPGIGQIIPLSEVPDQVFAGKMMGDGVGFIPEKGEIVAPFDGTVKTIFPTKHAIGLESESGVEVLIHIGIDTVKLNGEGFESLINVDEKVTQGQPLMKVNLAYLKAHAPSIVTPMIITNLENKELVIEDVQDADPGKLIMTVK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000255
EMBL· GenBank· DDBJ
ABD21359.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp