E3PJ86 · GSPD2_ECOH1

Function

function

Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable).

Miscellaneous

Encoded in a type II secretion system (T2SS-beta); this strain encodes 2 T2SS but only this one (beta) is expressed under standard laboratory conditions.

Features

Showing features for site.

168650100150200250300350400450500550600650
TypeIDPosition(s)Description
Site493May serve as a pivot that allows opening of the central gate for substrate egress

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 Componentcell outer membrane
Cellular Componenttype II protein secretion system complex
Biological Processprotein secretion by the type II secretion system

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Secretin GspD 2
  • Alternative names
    • General secretion pathway protein D 2 (GspD)
    • GspD-beta secretin
    • Type II secretion system protein D 2 (T2SS protein D)

Gene names

    • Name
      gspD2
    • Synonyms
      gspD-beta
    • Ordered locus names
      ETEC_3237

Organism names

Accessions

  • Primary accession
    E3PJ86

Subcellular Location

Cell outer membrane
Note: Some protein is also found in the cell inner membrane, the inner membrane protein does not form multimers and is unstable (PubMed:22585966).
Most of the protein is in the periplasm which it traverses to contact proteins of the cell inner membrane (Probable)

Keywords

Phenotypes & Variants

Disruption phenotype

Severely disrupts assembly and function of T2SS-beta.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis675-681Binds AspS2 normally.
Mutagenesis676Binds AspS2 normally.
Mutagenesis676-680No longer binds AspS2.
Mutagenesis679No longer binds AspS2, the AspS2-GspD2 complex no longer forms in vivo.
Mutagenesis680Binds AspS2 normally.
Mutagenesis684-686Binds AspS2 normally.

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-40
ChainPRO_500317963241-686Secretin GspD 2

Interaction

Subunit

Forms a cylindrical channel with 15 subunits, each of which interacts with the surrounding pilotin AspS2 proteins (also called GspS-beta) (PubMed:29632366).
Interacts with inner cell membrane protein GspC2 in the periplasm (PubMed:21931548).
Forms multimers in the outer membrane (PubMed:22585966).
The isolated N0 domain forms dimers that self-assemble into rings (PubMed:23820381).

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region41-140N0, contacts GspC2
Region142-206N1
Region207-279N2
Region282-357N3
Region360-627Secretin
Region414-433Cap gate
Region629-686S domain, contacts AspS2

Domain

The N0 region interacts in the periplasm with GspC (PubMed:21931548).
The S domain interacts with pilotin AspS2 (PubMed:29632366).
The N0, N1, N2 and N3 domains are periplasmic, while the secretin and S domains form a channel that is partially inserted in the outer membrane. The cap gate extends out on the extracellular side of the channel partially closing the channel. The secretin domain forms a double beta-barrel structure; the outer barrel has an outer diameter of about 110 Angstroms while the inner barrel forms the central gate with a small pore in the closed state (By similarity).

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    686
  • Mass (Da)
    74,202
  • Last updated
    2011-01-11 v1
  • Checksum
    213BE2A98A043B4F
MFWRDITLSVWRKKTTGLKTKKRLLPLVLAAALCSSPVWAEEATFTANFKDTDLKSFIETVGANLNKTIIMGPGVQGKVSIRTMTPLNERQYYQLFLNLLEAQGYAVVPMENDVLKVVKSSAAKVEPLPLVGEGSDNYAGDEMVTKVVPVRNVSVRELAPILRQMIDSAGSGNVVNYDPSNVIMLTGRASVVERLTEVIQRVDHAGNRTEEVIPLDNASASEIARVLESLTKNSGENQPATLKSQIVADERTNSVIVSGDPATRDKMRRLIRRLDSEMERSGNSQVFYLKYSKAEDLVDVLKQVSGTLTAAKEEAEGTVGSGREIVSIAASKHSNALIVTAPQDIMQSLQSVIEQLDIRRAQVHVEALIVEVAEGSNINFGVQWASKDAGLMQFANGTQIPIGTLGAAISQAKPQKGSTVISENGATTINPDTNGDLSTLAQLLSGFSGTAVGVVKGDWMALVQAVKNDSSSNVLSTPSITTLDNQEAFFMVGQDVPVLTGSTVGSNNSNPFNTVERKKVGIMLKVTPQINEGNAVQMVIEQEVSKVEGQTSLDVVFGERKLKTTVLANDGELIVLGGLMDDQAGESVAKVPLLGDIPLIGNLFKSTADKKEKRNLMVFIRPTILRDGMAADGVSQRKYNYMRAEQIYRDEQGLSLMPHTAQPVLPAQNQALPPEVRAFLNAGRTR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FN649414
EMBL· GenBank· DDBJ
CBJ02737.1
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